Crystal structure

ABSTRACT

The present invention relates to the soakable crystal structures of a phosphodiesterase 5 (PDE5) and their uses in identifying PDE5 ligands, including PDE5 inhibitor compounds. The present invention also relates to methods of identifying such PDE5 inhibitor compounds and their medical use. The present invention additionally relates to crystals of PDE5 into which ligands may be soaked and crystals of PDE5 comprising PDE5 ligands that have been soaked into the crystal.

RELATED APPLICATIONS AND PRIORITY CLAIMS THERETO

[0001] This application is a continuation-in-part of U.S. applicationNo. (Not yet determined), filed on Apr. 30, 2003, entitled “CrystalStructure” of Brown et. al. which is the National Stage Application ofInternational Application No. PC/IB02/04426 filed on Oct. 24, 2002,having designated the United States and published on (Not yetdetermined). The subject matter of the co-pending U.S. application No.(Not yet identified) and International Application No. GB/IB02/04426 isincorporated-by-reference in their entirety herein.

[0002] This application claims priority under 35 USC §119, 120 and 365to the following foreign patent applications: Application No. GB0126417.5 filed in the United Kingdom on Nov. 2, 2001, and InternationalApplication No. PC/IB02/04426 filed in the WO on Oct. 24, 2002 andhaving designated the U.S. as a receiving country.

TECHNICAL FIELD

[0003] The present invention relates to crystal structures of aphosphodiesterase 5 (PDE5) and ligand complexes of PDE5 and to theiruses in identifying PDE5 ligands, including PDE5 inhibitor compounds.The present invention also relates to methods of identifying such PDE5inhibitor compounds and their medical use. The present inventionadditionally relates to crystals of PDE5 into which ligands may besoaked and to crystals of PDE5 comprising ligands that have been soakedinto the crystal. Also contemplated by the present invention is the useof crystals of PDE5 into which ligands may be soaked in identifyingligands of PDE5, including PDE5 inhibitor compounds.

BACKGROUND OF THE INVENTION

[0004] A wide variety of biological processes, including cardiac musclecontraction, regulation of blood flow, neural transmission, glandularsecretion, cell differentiation and gene expression are affected bysteady state levels of the cyclic nucleotide biological secondmessengers cAMP and cGMP. Intracellular receptors for these moleculesinclude cyclic nucleotide dependent protein kinases (PGK) (Lohmann etal. 1997), cyclic nucleotide-gated channels, and class Iphosphodiesterases (PDEs) (Charbonneau 1990). PDEs are a large family ofproteins, which were first reported by Sutherland and co-workers (Rall &Sutherland 1958, Butcher & Sutherland 1962). The family of cyclicnucleotide phosphodiesterases catalyse the hydrolysis of 3′, 5′-cyclicnucleotides to the corresponding 5′ monophosphates. Current literatureshows that there are eleven related, but biochemically distinct, humanphosphodiesterase gene groups and that many of these groups include morethan one gene subtype giving a total of twenty genes. Some PDEs arehighly specific for hydrolysis of cAMP (PDE4, PDE7, PDE8), some arehighly cGMP specific (PDE5, PDE6, PDE9), and some have mixed specificity(PDE1, PDE2, PDE3, PDE10, PDE11). All PDEs are multi-domain proteins;each PDE has a˜270 amino acid domain located towards the C-terminus,which has a high degree of amino acid sequence conservation betweenfamilies (Charbonneau 1986). This domain has been extensively studiedand shown to be responsible for the common catalytic function (Francis,S. H. et al. 1994). Non-homologous segments in the remainder of theprotein have regulatory function or confer specific binding properties.PDE2, PDE5, PDE6 and PDE10 are all reported to contain putative GAFdomains within their regulatory amino terminal portion (Aravind &Ponting 1997 and Soderling & Beavo 2000). These GAF domains have beenshown to bind cGMP but their function is not yet fully understood. Fulllength mammalian PDEs characterised to date are dimeric in solution, butthe relevance of the dimeric structure is unknown. The structure of theregulatory segment of PDE2A bound to cGMP has recently been solved andreveals a parallel dimer of four GAF domains, with cGMP binding to onlyone of the two GAF domains on each monomer (Martinez, et al. 2001).

[0005] PDE5, a cGMP specific PDE, has been recognised in recent years asan important therapeutic target. It is composed of the conservedC-terminal, zinc containing, catalytic domain, which catalyses thecleavage of cGMP, and an N-terminal regulatory portion, which containstwo GAF domain repeats. Each GAF domain contains a cGMP-binding site,one of high affinity and the other of lower affinity. PDE5 activity isregulated through binding of cGMP to the high and low affinity cGMPbinding sites followed by phosphorylation, which occurs only when bothsites are occupied (Thomas et al. 1990). PDE5 is found in varyingconcentrations in a number of tissues including platelets, vascular andvisceral smooth muscle, and skeletal muscle. The protein is a keyregulator of cGMP levels in the smooth muscle of the erectile corpuscavernosal tissue. The physiological mechanism of erection involvesrelease of nitric oxide (NO) in the corpus cavernosum during sexualstimulation. NO then activates the enzyme guanylate cyclase, whichresults in increased levels of cGMP, producing smooth muscle relaxationin the corpus cavernosum and allowing in flow of blood. Inhibition ofPDE5 inhibits the breakdown of cGMP allowing the levels of cGMP, andhence smooth muscle relaxation, to be maintained (Corbin & Francis1999). Sildenafil (UK-092,480), the active ingredient of Viagra® and apotent inhibitor of PDE5, has attracted widespread attention for theeffective treatment of male erectile dysfunction.

[0006] Structural information has recently been shown for the catalyticdomain of PDE4b a cAMP-specific PDE (Xu et al. 2000). This structureprovides information about the overall fold of the catalytic domains ofthe PDE family, but, to date, no structural information is known aboutthe way in which potential inhibitors bind to the enzyme.

[0007] The X-ray structure of a recombinant PDE5 comprising thecatalytic domain in complex with Sildenafil has been determined (seeearlier related patent application Number PCT/EB02/04426: Example 9,“crystallisation of wild type PDE5 catalytic domain with Sildenafil”,page 44, line 29 to page 45, line 17; Example 13, “Data collection,structure determination and refinement of wild type PDE5 withSildenafil”, page 48, line 1 to page 49, line 9; Table 4, page 91 to248; incorporated herein by reference). An engineered form of this PDE5,PDE5*, which shows improved qualities for the production of crystals ofligand complexes, has also been produced and the structure of such acomplex has been determined (see Application Number PCT/IB02/04426:Example 11, “crystallisation of PDE5* with Sildenafil”, page 46, lines 8to 25; Example 15, “data collection, structure determination andrefinement of PDE5* with Sildenafil”, page 50, line 9 to page 51, line6; and Table 6, “atomic coordinates for baculovirus-expressed PDE5*complex with Sildenafil”, pages 328 to 408; incorporated herein byreference). These complexes not only provide important structuralinformation about this novel family of proteins but also assist thedesign of more potent and specific inhibitors of PDEs to treat the manydiseases where PDEs play a role.

[0008] It is desirable to be able to obtain crystals of biologicalmacromolecules in a complex with their ligands in order to obtaindetails of specific ligand interactions at a level of molecularresolution and, preferably, at atomic resolution. This invariably formsthe critical step in providing information from which further, andpossibly improved, ligands of the macromolecule may be designed andsubsequently tested in further rounds of crystallisation. It istherefore most desirable that this process of obtaining complexes of themacromolecule be rapid and reproducible and minimise the need toconstantly find new crystallisation conditions for each potentialcomplex or use involved and time intensive structure solution methodsfor the solution of each potential complex structure. To this end themost desirable crystal form of a macromolecule of interest is one whichis amenable to having potential ligands soaked into the preformedcrystal of the apo macromolecule. This has distinct advantages overconventionally produced co-crystals. In particular no newcrystallisation conditions need to be found for each potential complex.The lattice symmetry and cell dimensions for each new ligand complexwill be substantially the same as for the apo macromolecule such thatthe data collection parameters for the apo and all complex crystals willessentially be identical. The structure solution can then occur usingrapid difference fourier methods, thus avoiding more involved time andlabour intensive phasing methods. Consequently, soakable crystals ofmacromolecules allow for particularly rapid screening and structuraldetermination of new macromolecule-ligand complexes.

[0009] The engineered form of PDE5, PDE5*, allows the production ofsoakable crystals of ligand complexes, and the structure of such asoaked PDE5*-ligand complex has been determined.

SUMMARY OF THE INVENTION

[0010] It has been found that PDE5 can be crystallised. It has also beenfound that manipulating the wild-type PDE5 amino acid sequence canfacilitate the crystallisation of PDE5. Specifically, it has been foundthat manipulations of certain portions of the PDE5 amino acid sequencecan facilitate the crystallisation of PDE5. More specifically it hasbeen shown that particular manipulations of the PDE5 amino acid sequencecan provide soakable crystal forms of PDE5 into which potential PDE5ligands may be introduced by the process of crystal soaking.

[0011] It has been shown that manipulations of the catalytic domain ofPDE5, specifically the 657-682 region of PDE5 (the “loop region”), canfacilitate the crystallisation of PDE5 and particularly provide soakablecrystals of PDE5. More specifically, manipulations of the loop regionamino acid sequence (HRGVNNSYIQRSEHPLAQLYCHSIME=SEQ ID NO: 1) of PDE5can facilitate the crystallisation of PDE5 and provide soakable crystalsof PDE5. This manipulation can be achieved by deletion, addition orsubstitution of one or more amino acid residues of the PDE5 loop regionor it can be achieved by complete replacement of the PDE5 loop regionwith a loop region (or other amino acid sequence) from another protein,preferably another PDE, more preferably PDE4, most preferably PDE4b.

[0012] Crystals of PDE5 have been found to be useful for screening forPDE5 ligands, especially PDE5 inhibitors by (i) co-crystallising PDE5with the PDE5 ligand (e.g. PDE5 inhibitor), as shown in ApplicationNumber PCT/IB02/04426 (Example 9, “crystallisation of wild type PDE5catalytic domain with Sildenafil”, page 44, line 29 to page 45, line 17;Example 11, “crystallisation of PDE5* with Sildenafil”, page 46, lines 8to 25; Example 13, “Data collection, structure determination andrefinement of wild type PDE5 with Sildenafil”, page 48, line 1 to page49, line 9; Example 15, “data collection, structure determination andrefinement of PDE5* with Sildenafil”, page 50, line 9 to page 51, line6; Table 4 “atomic co-ordinates for wild type PDE5 complexed withSildenafil”, pages 91 to 240; and Table 6, “atomic co-ordinates forbaculovirus—expressed PDE5* complex with Sildenafil”, pages 328 to 408;incorporated herein by reference), or (ii) by soaking the PDE5 ligand(e.g. PDE5 inhibitor) into the crystal of PDE5, as shown in the presentinvention.

[0013] PDE5 ligands, especially PDE5 inhibitors, as identified by themethods of the present invention are useful in curative, palliative orprophylactic treatments.

[0014] Thus, the present invention provides the following (numbered)aspects:

ASPECTS

[0015] 1. A crystal of phosphodiesterase 5 (PDE5), wherein the crystalis soakable.

[0016] 2. The crystal of PDE5 according to aspect 1, wherein said PDE5is from a mammal.

[0017] 3. The crystal of PDE5 according to aspect 1 or aspect 2, whereinsaid PDE5 is from a human.

[0018] 4. The crystal of PDE5 according to any one of aspects 1 to 3,wherein said PDE5 is an isoform selected from the group consisting ofPDE5A1, PDE5A2, PDE5A3 and PDE5A4.

[0019] 5. The crystal of PDE5 according to any one of aspects 1 to 4,wherein said PDE5 comprises SEQ ID NO: 1 (PDE5 loop region) or ahomologue, fragment, variant, analogue or derivative thereof.

[0020] SEQ ID NO: 1 is the so-called “loop region” of PDE5. This loopregion or a homologue, fragment, variant, analogue or derivative thereofincludes additions, deletions or substitutions of amino acid residuescomprised within the loop region.

[0021] Preferably, a variant in relation to the amino acid sequence ofthe crystal of the PDE5 of the present invention includes the deletionor substitution of the histidine (His/H) residue as shown emboldened andunderlined in SEQ ID NO: 1 (HRGVNNSYIQRSEHPLAQLYCHSIME). Replacement ofsaid histidine (H) residue is preferably by way of incorporating one ormore amino acid residues (other than histidine), preferably wherein saidamino acid residues are neutral or non-polar.

[0022] More preferably, a variant in relation to the amino acid sequenceof the crystal of the PDE5 of the present invention includes thecomplete replacement of the loop region with a loop region (or otheramino acid sequence) from another protein, preferably a PDE, morepreferably PDE4, most preferably PDE4b (see hereinafter).

[0023] 6. The crystal of PDE5 according to any one of aspects 1 to 5,wherein said PDE5 comprises SEQ ID NO: 4 (PDE4 loop) or a homologue,fragment, variant, analogue or derivative thereof.

[0024] 7. The crystal of PDE5 according to any one of aspects 1 to 6,wherein said PDE5 comprises SEQ ID NO: 5 (PDE5*=loop swapped PDE5catalytic domain) or a homologue, fragment, variant, analogue orderivative thereof

[0025] 8. The crystal of PDE5 according to any one of aspects 1 to 7,wherein said PDE5 comprises SEQ ID NO: 6 (full PDE5 sequence comprisingPDE5*) or a homologue, fragment, variant, analogue or derivativethereof.

[0026] 9. The crystal of PDE5 according to any of the preceding aspectswhich is grown using polyethylene glycol as a precipitant. Polyethyleneglycol of molecular weights 2000 to 8000 are commonly used. Preferablythe molecular weight of the polyethylene glycol is 4000. Thepolyethylene glycol may be at a concentration of between 10% and 30%,but is most preferably 20%. Additionally, the PDE5 protein used to growthe crystals is desired to be of a concentration between 1 and 20 mg/ml,preferably between 5 and 15 mg/ml and most preferably is at 10 mg/mlconcentration.

[0027] 10. The crystal of PDE5 according to any of the preceding aspectswhich is grown in a buffer in the pH range of 6.5 to 8.0. Preferably thepH is in the range of 7.0 to 7.8; most preferably the pH is 7.4. Thebuffer should be one capable of providing buffer capacity over therequired pH range, preferably HEPES.

[0028] 11. The crystal of PDE5 according to any of the preceding aspectswhich is grown in the presence of an alcohol. Preferably the alcohol isisopropanol.

[0029] 12. The crystal of PDE5 according to any of the preceding aspectswhich is grown in a solution containing HEPES buffer, polyethyleneglycol 4000 and iso-propanol. Preferably the solution contains 0.1Msodium HEPES pH 7.4, 20% polyethylene glycol 4000 and 10% iso-propanol.The crystal is grown from solution inclubated at or below roomtemperature (20-25° C.). Preferably the crystal is grown from a solutioninclubated at a temperature within the range of 2-6° C. More preferably,the crystal is grown from a solution inclubated at about 4° C.

[0030] Soakable crystals may be grown using a variety of methods such asdialysis, sitting drop vapour diffusion or batch methods,microcrystallisation methods, micro or macro seeding methods or gelcrystallisation methods but are preferably grown using hanging dropvapour diffusion.

[0031] 13. The crystal of PDE5 as defined in any of the precedingaspects, which has one or more of the following characteristics:

[0032] (a) a space group C2;

[0033] (b) unit cell dimensions a˜56 Å±1%, b˜77 Å±1%, c˜81Å±1%, α=y=90°,β=103°±1%;

[0034] (c) 1 molecule per asymmetric unit;

[0035] (d) comprises a PDE5 of a molecular weight of approximately 40kDa±2 kDa;

[0036] (e) a calculated solvent content of approximately 47±5%; and

[0037] (f) a monoclinic crystal system.

[0038] 14. The crystal of PDE5 according to any of the precedingaspects, wherein PDE5 has an active site within the third sub-domain ofthe protein which is bounded by Helices 15 (H15 813-824) and 14 (H14772-797), the C-terminus of Helix 13 (H13 749-765), and the C-terminusof Helix 11 (H11 706-721) along with the loop region between Helices 11and 12a (H12a 725-731) as shown in FIG. 2.

[0039] 15. The crystal of PDE5 according to aspect 14, wherein theactive site is capable of accommodating a pyrazolo-pyrimidinone. Anexample of a preferred pyrazolo-pyrimidinone is UK-088,800. Anotherexample of a pyrazolo-pyrimidinone is Sildenafil.

[0040] UK-088,800 is illustrated in FIG. 4 and is a structuralrepresentation of the compound with the chemical name5-(2-ethoxyphenyl)-1-methyl-3-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one.

[0041] 16. The crystal of PDE5 according to any of the precedingaspects, wherein PDE5 has an active site within the third sub-domain ofthe protein and comprises Leu 765, Ala 767 and Ile 768 and one or moreof Phe 820, Val 782, Phe 786, Tyr 612, Leu 804, Ala 779, Ala 783, Ile813, Met 816 and Gln 817.

[0042] 17. The crystal of PDE5 according to aspect 16, wherein theactive site is capable of accommodating a pyrazolo-pyrimidinone. Anexample of a preferred pyrazolo-pyrimidinone is UK-088,800. Anotherexample of a pyrazolo-pyrimidinone is Sildenafil.

[0043] 18. The crystal of PDE5 according to any of the precedingaspects, wherein said PDE5 has a three-dimensional structurecharacterised by the atomic co-ordinates set out in Table 4 (PDE5* apoC2 form) or a derivative set as expressed in any reference frame.

[0044] 19. A heavy atom derivative of the crystal of PDE5 according toany of the preceding aspects.

[0045] 20. The crystal of PDE5 according to any of the precedingaspects, wherein a PDE5 ligand has been soaked in. The process ofsoaking may involve transferring the crystal to be soaked from thesolution in which it is grown into a stabilising solution containing theligand or to which the ligand is to be added once the crystal is presentin it. It is desirable that the stabilising solution has the physicalproperties such that the crystal, when transferred, retains itsstructural integrity and does not crack or dissolve or altersignificantly in its crystal parameters, symmetry or cell dimensions..Preferably, the stabilising solution comprises some or all of thechemical constituents from which the crystal was grown. More preferably,the stabilising solution is of similar or identical composition to thesolutions used for crystal growth as set out in aspects 9 to 12 above,although the concentration of precipitant used may be slightlyincreased. Most preferably the stabilising solution has the same pH asthe crystal growth solution. The ligand may be added to the solutioncontaining, or to contain, the crystal for soaking as a solid or in aliquid form (i.e. the ligand already being in solution). Preferably theligand is in solution and the solvent maybe aqueous, organic ornon-organic. Most preferably the ligand is in DMSO. The ligand iscommonly added to the soaking solution to yield a final ligandconcentration above the expected binding constant for the ligand byPDE5; preferably this is greater than or equal to 10 times the bindingconstant. The final concentration of ligand present in the crystalsoaking solution is preferably between 0.1 and 20 mg/ml, more preferablybetween 0.5 and 10 mg/ml, and most preferably between 1 and 5 mg/ml.

[0046] 21. The crystal of PDE5 according to aspect 20, wherein said PDE5ligand is a PDE5 inhibitor.

[0047] 22. The crystal of PDE5 according to aspect 21, wherein said PDE5inhibitor is a pyrazolo-pyrimidinone, preferably UK-088,800.Alternatively the inhibitor is Sildenafil.

[0048] 23. The crystal of PDE5 according to aspect 22, wherein said PDE5has a three-dimensional structure characterised by the atomicco-ordinates set out in Table 5 (PDE5*-UK-088,800 complex) or aderivative set as expressed in any reference frame.

[0049] 24. Use of the atomic co-ordinates determined from the crystal ofPDE5 according to any one of the preceding aspects for deriving athree-dimensional structure of a PDE5 or a mutant, derivative, variant,analogue, homologue, sub-domain or fragment thereof.

[0050] 25. Use according to aspect 24, wherein the PDE5 sub-domain isthe catalytic domain.

[0051] 26. Use of the three-dimensional structure of PDE5 as derivableaccording to aspect 24 or aspect 25 to computationally or otherwiseevaluate the binding interactions of a chemical compound with an activesite on PDE5.

[0052] 27. Use of the three-dimensional structure of PDE5 as derivableaccording to aspect 26 to design a compound capable of associating withPDE5. Preferably said compound is a pyrazolo-pyrimidinone, morepreferably UK-088,800. Alternatively the compound is Sildenafil.

[0053] 28. Use according to aspect 26 or aspect 27, wherein the compoundis a PDE5 ligand.

[0054] 29. Use according to aspect 28, wherein said compound is a PDE5inhibitor.

[0055] 30. Use according to aspect 29, wherein said PDE5 inhibitor is apyrazolo-pyrimidinone, preferably UK-088,800. Alternatively theinhibitor is Sildenafil.

[0056] 31. A method of selecting a compound capable of associating withPDE5 from a group of potential PDE5 ligand compounds comprising thefollowing steps:

[0057] i. soaking the crystal of PDE5 according to any one of aspects 1to 19 in a solution containing a potential PDE5 ligand compound;

[0058] ii. determining the three-dimensional structure from the soakedcrystal; and

[0059] iii. assessing whether the compound is bound to PDE5.

[0060] 32. A compound selected by the use according to aspect 31.

[0061] 33. A compound designed by the use according to any one ofaspects 27 to 30 or identified by the method of aspect 31.

[0062] 34. The compound according to aspect 33, which is a PDE5inhibitor.

[0063] 35. A method of selecting a PDE5 ligand from a group of potentialPDE5 ligands, comprising the following steps:

[0064] (a) computationally creating a three-dimensional representationof the structure of PDE5 as derivable according to aspect 24 or aspect25, and a three-dimensional representation of the structure of thepotential PDE5 ligand;

[0065] (b) co-displaying the three-dimensional representation of thepotential PDE5 ligand with the three-dimensional representation of thePDE5 structure; and

[0066] (c) assessing whether the three-dimensional representation of thepotential PDE5 ligand fits the three-dimensional representation of anactive site of the PDE5 structure.

[0067] Preferably, ligands are built using molecular graphics tools,more preferably the designed ligand is energy minimised prior toco-display and analysis.

[0068] 36. The method according to aspect 35, further comprising thefollowing steps:

[0069] (d) incorporating the potential PDE5 ligand in a biological PDE5activity assay; and

[0070] (e) determining whether the potential PDE5 ligand modulates PDE5activity in said assay.

[0071] 37. The method according to aspect 35 or aspect 36 wherein saidpotential PDE5 ligand is a potential PDE5 inhibitor compound and saidpotential PDE5 inhibitor compound inhibits PDE5 activity.

[0072] 38. A PDE5 ligand selected by the method of any one of aspects 35to 37. Preferably the ligand is a PDE5 inhibitor.

[0073] 39. Use of a PDE5 ligand according to aspect 38 as apharmaceutical. Preferably the ligand is a PDE5 inhibitor.

[0074] 40. A pharmaceutical composition comprising one or more PDE5ligands according to aspect 38 and one or more pharmaceuticallyacceptable excipients.

[0075] 41. Use of a PDE5 ligand according to aspect 38 in themanufacture of a medicament for the prophylaxis or treatment of acondition, disease, disorder or dysfunction where the inhibition of PDE5is prophylactically or therapeutically beneficial.

[0076] 42. Use according to aspect 41, wherein said disorder is amammalian sexual disorder.

[0077] The curative, palliative or prophylactic treatments contemplatedby the present invention include the curative, palliative orprophylactic treatment of mammalian sexual disorders, in particular thetreatment of mammalian sexual dysfunctions such as male erectiledysfunction (MED), impotence, female sexual dysfunction (FSD), clitoraldysfunction, female hypoactive sexual desire disorder, female sexualarousal disorder (FSAD), female sexual pain disorder or female sexualorgasmic dysfunction (FSOD) as well as sexual dysfunction due to spinalcord injury or selective serotonin re-uptake inhibitor (SSRI) inducedsexual dysfunction but, clearly, will also be useful for treating othermedical conditions for which PDE5 inhibitor is indicated. Suchconditions include premature labour, dysmenorrhoea, benign prostatichyperplasia (BPH), bladder outlet obstruction, incontinence, stable,unstable and variant (Prinzmetal) angina, hypertension, pulmonaryhypertension, chronic obstructive pulmonary disease, coronary arterydisease, congestive heart failure, atherosclerosis, conditions ofreduced blood vessel patency, e.g. post-percutaneous transluminalcoronary angioplasty (post-PTCA), peripheral vascular disease, stroke,nitrate induced tolerance, bronchitis, allergic asthma, chronic asthma,allergic rhinitis, diseases and conditions of the eye such as glaucoma,optic neuropathy, macular degeneration, elevated intra-occular pressure,retinal or arterial occulsion and diseases characterised by disorders ofgut motility, e.g. irritable bowel syndrome (IBS).

[0078] Further medical conditions for which a PDE5 inhibitor isindicated, and for which treatment with compounds of the presentinvention may be useful include pre-eclampsia, Kawasaki's syndrome,nitrate tolerance, multiple sclerosis, diabetic nephropathy, neuropathyincluding autonomic and peripheral neuropathy and in particular diabeticneuropathy and symptoms thereof e.g. gastroparesis, peripheral diabeticneuropathy, Alzheimer's disease, acute respiratory failure, psoriasis,skin necrosis, cancer, metastasis, baldness, nutcracker oesophagus, analfissure, haemorrhoids, the insulin resistance syndrome, diabetes,hypoxic vasoconstriction as well as the stabilisation of blood pressureduring haemodialysis.

[0079] Particularly preferred conditions include MED and FSD (preferablyFSAD).

[0080] Further (numbered) aspects of the present invention include:

[0081] 43. Use of the atomic co-ordinates determined from the crystal ofPDE5 according to any one of aspects 1 to 23, to solve the crystalstructure of a mutant, derivative, fragment, variant, analogue,homologue or complex of PDE5.

[0082] 44. Use of the atomic co-ordinates determined from the crystal ofPDE5 according to any one of aspects 1 to 23, to produce a model of thethree-dimensional structure of PDE5-related proteins.

[0083] 45. Use of the three-dimensional structure of PDE5 as derivableaccording to aspect 24 or aspect 25 to design site-directed mutants thatmimic other PDE5 isoforms or variants thereof.

[0084] 46. A method of soaking a chemical compound into a crystalaccording to any one of aspects 1 to 19 comprising the following steps:

[0085] a) incubating the crystal in an aqueous stabilising solutioncomprising buffer and polyethylene glycol;

[0086] b) combining the chemical compound with the stabilising solutionpreferably wherein the chemical compound is in solid or liquid form,more preferably in liquid form, most preferably solublised in DMSO; and

[0087] c) optionally adding a cryo-protectant to the stabilisingsolution.

[0088] 47. A method according to aspect 46, wherein the stabilisingsolution comprises polyethylene glycol which is of the molecular weight4000. The polyethylene glycol may be at a concentration of between 10%and 30%, but is most preferably 20%. Additionally the pH is preferablyin the range of 7.0 to 7.8; most preferably the pH is 7.4. The buffershould be one capable of providing buffer capacity over the required pHrange; preferably HEPES. Preferably the stabilising solution contains analcohol; most preferably this is isopropanol. Preferably the stabilisingsolution contains 0.1 M sodium HEPES pH 7.4, 20% polyethylene glycol4000 and 10% iso-propanol. Examples of suitable cryoprotectants include2-methyl-2,4-pentanediol (MPD) and organic polymers e.g. lower molecularweight PEG. Carbohydrates such as sorbitol or xylitol, and alcohols mayalso be used. Preferably the cryoprotectant is glycerol.

[0089] A PDE5 ligand (also known as a PDE5 inhibitor compound) accordingto aspect 38 (hereinafter referred to as “the compound”) can beadministered alone but, in human therapy, will generally be administeredin admixture with a suitable pharmaceutical excipient diluent or carrierselected with regard to the intended route of administration andstandard pharmaceutical practice. Thus, the pharmaceutical compositions,pharmaceuticals and medicaments contemplated by the present inventionmay be formulated in various ways well-known to one of skill in the artand administered by similarly well-known methods.

[0090] For example, the compound of the invention can be administeredorally, buccally or sublingually in the form of tablets, capsules(including soft gel capsules), ovules, elixirs, solutions orsuspensions, which may contain flavouring or colouring agents, forimmediate-, delayed-, modified-, or controlled-release such assustained-, dual-, or pulsatile delivery applications. The compound mayalso be administered via intracavemosal injection. The compound may alsobe administered via fast dispersing or fast dissolving dosages forms orin the form of a high-energy dispersion or as coated particles. Suitablepharmaceutical formulations of the compound may be in coated orun-coated form as desired.

[0091] Such tablets may contain excipients such as microcrystallinecellulose, lactose, sodium citrate, calcium carbonate, dibasic calciumphosphate, glycine and starch (preferably corn, potato or tapiocastarch), disintegrants such as sodium starch glycollate, croscarmellosesodium and certain complex silicates, and granulation binders such aspolyvinylpyrrolidone, hydroxypropylmethyl cellulose (HPMC),hydroxypropylcellulose (HPC), sucrose, gelatin and acacia. Additionally,lubricating agents such as magnesium stearate, stearic acid, glycerylbehenate and talc may be included.

[0092] Solid compositions of a similar type may also be employed asfillers in gelatin capsules. Preferred excipients in this regard includelactose, starch, a cellulose, milk sugar or high molecular weightpolyethylene glycols. For aqueous suspensions and/or elixirs, thecompound may be combined with various sweetening or flavouring agents,colouring matter or dyes, with emulsifying and/or suspending agents andwith diluents such as water, ethanol, propylene glycol and glycerin, andcombinations thereof.

[0093] Modified release and pulsatile release dosage forms may containexcipients such as those detailed for immediate release dosage formstogether with additional excipients that act as release rate modifiers,these being coated on and/or included in the body of the device. Releaserate modifiers include, but are not exclusively limited to,hydroxypropylmethyl cellulose, methyl cellulose, sodiumcarboxymethylcellulose, ethyl cellulose, cellulose acetate, polyethyleneoxide, Xanthan gum, Carbomer, ammonio methacrylate copolymer,hydrogenated castor oil, carnauba wax, paraffin wax, cellulose acetatephthalate, hydroxypropylmethyl cellulose phthalate, methacrylic acidcopolymer and mixtures thereof. Modified release and pulsatile releasedosage forms may contain one or a combination of release rate modifyingexcipients. Release rate-modifying excipients maybe present both withinthe dosage form i.e. within the matrix, and/or on the dosage form i.e.upon the surface or coating.

[0094] Fast dispersing or dissolving dosage formulations (FDDFs) maycontain the following ingredients: aspartame, acesulfame potassium,citric acid, croscarmellose sodium, crospovidone, diascorbic acid, ethylacrylate, ethyl cellulose, gelatin, hydroxypropylmethyl cellulose,magnesium stearate, mannitol, methyl methacrylate, mint flavouring,polyethylene glycol, fumed silica, silicon dioxide, sodium starchglycolate, sodium stearyl fumarate, sorbitol, xylitol. The termsdispersing or dissolving as used herein to describe FDDFs are dependentupon the solubility of the drug substance used i.e. where the drugsubstance is insoluble a fast dispersing dosage form can be prepared andwhere the drug substance is soluble a fast dissolving dosage form can beprepared.

[0095] The compound can also be administered parenterally, for example,intracavernosally, intravenously, intra-arterially, intraperitoneally,intrathecally, intraventricularly, intraurethrally intrasternally,intracranially, intramuscularly or subcutaneously, or they may beadministered by infusion or needleless injection techniques. For suchparenteral administration they are best used in the form of a sterileaqueous solution which may contain other substances, for example, enoughsalts or glucose to make the solution isotonic with blood. The aqueoussolutions should be suitably buffered (preferably to a pH of from 3 to9), if necessary. The preparation of suitable parenteral formulationsunder sterile conditions is readily accomplished by standardpharmaceutical techniques well-known to those skilled in the art.

[0096] For oral and parenteral administration to human patients, thedaily dosage level of the compound will usually be from 10 to 500 mg (insingle or divided doses).

[0097] Thus, for example, tablets or capsules of the compound maycontain from 5 mg to 250 mg of active compound for administration singlyor two or more at a time, as appropriate. The physician in any eventwill determine the actual dosage which will be most suitable for anyindividual patient and it will vary with the age, weight and response ofthe particular patient. The above dosages are exemplary of the averagecase. There can, of course, be individual instances where higher orlower dosage ranges are merited and such are within the scope of thisinvention. The skilled person will also appreciate that, in thetreatment of certain conditions (including MED and FSD), the compoundmay be taken as a single dose on an “as required” basis (i.e. as neededor desired).

[0098] The compound can also be administered intranasally or byinhalation and are conveniently delivered in the form of a dry powderinhaler or an aerosol spray presentation from a pressurised container,pump, spray or nebuliser with the use of a suitable propellant, e.g.dichlorodifluoromethane, trichlorofluoromethane,dichlorotetrafluoroethane, a hydrofluoroalkane such as1,1,1,2-tetrafluoroethane (HFA 134A™ or 1,1,1,2,3,3,3-heptafluoropropane(HFA 227EA™), carbon dioxide or other suitable gas. In the case of apressurised aerosol, the dosage unit may be determined by providing avalve to deliver a metered amount. The pressurised container, pump,spray or nebuliser may contain a solution or suspension of the activecompound, e.g. using a mixture of ethanol and the propellant as thesolvent, which may additionally contain a lubricant, e.g. sorbitantrioleate. Capsules and cartridges (made, for example, from gelatin) foruse in an inhaler or insufflator may be formulated to contain a powdermix of a compound of the invention and a suitable powder base such aslactose or starch.

[0099] Aerosol or dry powder formulations are preferably arranged sothat each metered dose or “puff” contains from 1 to 50 mg of a compoundof the invention for delivery to the patient. The overall daily dosewith an aerosol will be in the range of from 1 to 50 mg which may beadministered in a single dose or, more usually, in divided dosesthroughout the day.

[0100] The compound may also be formulated for delivery via an atomiser.Formulations for atomiser devices may contain the following ingredientsas solubilisers, emulsifiers or suspending agents: water, ethanol,glycerol, propylene glycol, low molecular weight polyethylene glycols,sodium chloride, fluorocarbons, polyethylene glycol ethers, sorbitantrioleate, oleic acid.

[0101] Alternatively, the compound can be administered in the form of asuppository or pessary, or they may be applied topically in the form ofa gel, hydrogel, lotion, solution, cream, ointment or dusting powder.The compound may also be dermally administered. The compound may also betransdermally administered, for example, by the use of a skin patch. Thecompound may also be administered by the ocular, pulmonary or rectalroutes.

[0102] For ophthalmic use, the compound can be formulated as micronisedsuspensions in isotonic, pH adjusted, sterile saline, or, preferably, assolutions in isotonic, pH adjusted, sterile saline, optionally incombination with a preservative such as a benzylalkonium chloride.Alternatively, the compound may be formulated in an ointment such aspetrolatum.

[0103] For application topically to the skin, the compound of theinvention can be formulated as a suitable ointment containing the activecompound suspended or dissolved in, for example, a mixture with one ormore of the following: mineral oil, liquid petrolatum, white petrolatum,propylene glycol, polyoxyethylene polyoxypropylene compound, emulsifyingwax and water. Alternatively, it can be formulated as a suitable lotionor cream, suspended or dissolved in, for example, a mixture of one ormore of the following: mineral oil, sorbitan monostearate, apolyethylene glycol, liquid paraffin, polysorbate 60, cetyl esters wax,cetearyl alcohol, 2-octyldodecanol, benzyl alcohol and water.

[0104] The compound may also be used in combination with a cyclodextrin.Cyclodextrins are known to form inclusion and non-inclusion complexeswith drug molecules. Formation of a drug-cyclodextrin complex may modifythe solubility, dissolution rate, bioavailability and/or stabilityproperty of a drug molecule. Drug-cyclodextrin complexes are generallyuseful for most dosage forms and administration routes. As analternative to direct complexation with the drug the cyclodextrin may beused as an auxiliary additive, e.g. as a carrier, diluent orsolubiliser. Alpha-, beta- and gamma-cyclodextrins are most commonlyused and suitable examples are described in WO-A-91/11172, WO-A-94/02518and WO-A-98/55148.

[0105] Generally, in humans, oral administration the compound is thepreferred route, being the most convenient and, for example in MED,avoiding the well-known disadvantages associated with intracavernosal(i.c.) administration. A preferred oral dosing regimen in MED for atypical man is from 25 to 250 mg of compound when required. Incircumstances where the recipient suffers from a swallowing disorder orfrom impairment of drug absorption after oral administration, the drugmay be administered parenterally, sublingually or buccally.

[0106] For veterinary use, the compound, or a veterinarily acceptablesalt thereof, or a veterinarily acceptable solvate or pro-drug thereof,is administered as a suitably acceptable formulation in accordance withnormal veterinary practice and the veterinary surgeon will determine thedosing regimen and route of administration which will be mostappropriate for a particular animal.

DETAILED DESCRIPTION OF THE INVENTION

[0107] The term “apo” as used herein is taken to mean macromolecule andinparticular any protein (or named protein) that is detached from a/itsligand(s) and/or prosthetic group(s).

[0108] The term “buffer” as used herein is taken to include any solutioncontaining a weak acid and a conjugate base of this acid (or, lesscommonly, a weak base and its conjugate acid). Thus, a “buffer” as usedherein resists change in its pH level when an acid or a base is added toit, because the acid neutralises an added base (or, less commonly, thebase neutralises an added acid).

[0109] An “activity assay” as referred to herein with reference to PDE5is taken to mean an in vitro assay of PDE inhibitory activities againstcyclic guanosine 3′,5′-monophosphate (cGMP) and cyclic adenosine3′,5′-monophosphate (cAMP) phosphodiesterases which can be determined bymeasurement of their IC₅₀ values (the concentration of compound requiredfor 50% inhibition of enzyme activity). Preferably the required PDEenzymes can be isolated from a variety of sources, including humancorpus cavemosum, human and rabbit platelets, human cardiac ventricle,human skeletal muscle and bovine retina, essentially by a modificationof the method of Thompson W J and Appleman M M; Biochemistry10(2),311-316, 1971, as described by Ballard S A et al.; J. Urology159(6), 2164-2171, 1998. In particular, cGMP-specific PDE5 andcGMP-inhibited cAMP PDE3 can be obtained from human corpus cavemosumtissue, human platelets or rabbit platelets.

[0110] Assays can be performed either using a modification of the“batch” method of Thompson, W J et al.; Biochemistry 18(23), 5228-5237,1979, essentially as described by Ballard S A et al.; J. Urology 159(6),2164-2171, 1998, or using a scintillation proximity assay for the directdetection of [³H]-labelled AMP/GMP using a modification of the protocoldescribed by Amersham plc under product code TRKQ7090/7100. In summary,for the scintillation proximity assay, the effect of PDE inhibitors areinvestigated by assaying a fixed amount of enzyme in the presence ofvarying inhibitor concentrations and low substrate (cGMP or cAMP in a3:1 ratio unlabelled to [³H]-labeled at a concentration of ˜⅓ K_(m) orless), such that IC₅≅K_(i). The final assay volume is made up to 100 μlwith assay buffer [20 mM Tris-HCl pH 7.4, 5mM MgCl₂, 1 mg/ml bovineserum albumin]. Reactions are initiated with enzyme, incubated for30-60min at 30° C. to give <30% substrate turnover and terminated with50 μl yttrium silicate SPA beads (containing 3 mM of the respectiveunlabelled cyclic nucleotide for PDE5). Plates are re-sealed and shakenfor 20 min, after which the beads are allowed to settle for 30 min inthe dark and then counted on a TopCount plate reader (Packard, Meriden,Conn.). Radioactivity units are converted to % activity of anuninhibited control (100%), plotted against inhibitor concentration, andinhibitor IC₅₀ values obtained using the ° Fit Curve Microsoft Excelextension.

[0111] The term “precipitant” as used herein is taken to include anysubstance that, when added to solution comprising a biological molecule,causes the biological molecule to precipitate or crystallise from thesolution.

[0112] The term “complex” as used herein is taken to mean a biologicalmacromolecule, preferably a protein, with ligand(s) bound and may beformed before, during or after protein crystallisation.

[0113] The term “soaking” as used herein is taken to mean a process ofplacing a crystal in an aqueous solution containing a chemical compound,(usually) small molecule (e.g. inhibitor), or adding a chemical compoundto an aqueous solution containing a crystal such that the compound maybe able to enter the crystal lattice by diffusion and may interact (e.g.contact and bond with) with the molecules comprising the latticepreferably to form a protein-ligand complex. The compound may be addedto the aqueous solution in solid form, or it may be dissolved in asuitable solvent, preferably di-methyl-sulphoxide (DMSO).

[0114] The term “soakable crystal” as used herein is taken to mean acrystal into which a small molecule or ligand may be soaked withoutsignificant disruption of the lattice such that the ligand can enter andpass through the crystal lattice and have access to, and may associatewith, the molecules comprising the lattice. Preferably a soakablecrystal is a crystal which is ameanable to the soaking process in whicha small molecule or ligand either in solution or in solid form is addedto the solution containing the crystal. The small molecule may thenenter the crystal lattice by diffusion and associate with the moleculescomprising the crystal lattice. It is preferable that the soakablecrystal binds the ligand without disruption of the lattice or crackingof the crystal and that the lattice symmetry and crystal parameters arenot significantly altered by the soaking and ligand binding process. Itis preferable that the soakable crystal diffracts X-rays to atomicresolution, preferably to beyond 3.5 Å, more preferably beyond 2.5 Å,most preferably 1.5 Å, after undergoing the soaking process.

[0115] The term “stabilising solution” as used herein is taken to mean asolution into which a crystal may be transferred for the purposes offurther manipulation, for example for soaking, and in which the crystalretains its structural integrity and does not crack or dissolve or altersignificantly in its crystal parameters, symmetry or cell dimensions.Preferably the stabilising solution comprises some or all of thechemical constituents from which the crystal was grown and is of theapproximately the same, and more preferably identical, pH.

[0116] The term “cryoprotectant” as used herein is taken to mean achemical compound which, when added to a solution, allows the solutionto be rapidly frozen without the formation of ice crystals. Such acryoprotectant is preferably an alcohol such as ethanol or acarbohydrate such as xylitol or sorbitol, but may also be2-methyl-2,4-pentanediol (MPD) or other organic polymers e.g. lowermolecular weight PEG. Most preferably the cryoprotectant is glycerol.

[0117] The term “co-crystallisation” as used herein is taken to meancrystallisation of a pre-formed comple of a macromolecule with it'sligand i.e. a protein/small molecule complex.

[0118] The terms “mutant”, “variant”, “homologue”, “analogue”,“derivative” or “fragment”, are in relation to the amino acid sequenceof the PDE5 protein or polypeptide sequence which is used to produce thecrystal of the present invention. The terms include any substitution of,variation of, modification of, replacement of, deletion of, or additionof one (or more) amino acids from (or to) the sequence providing theresultant PDE5 is capable of being crystallised.

[0119] Typically, for the “mutant”, “variant”, “homologue”, “analogue”,“derivative” or “fragment” in relation to the amino acid sequence of theprotein or polypeptide of the PDE5 of the crystal of the presentinvention, the types of amino acid substitutions that could be madeshould maintain the hydrophobicity/hydrophilicity of the amino acidsequence. Amino acid substitutions may be made, for example from 1, 2 or3 to 10, 20 or 30 substitutions, provided that the modified PDE5 retainsthe ability to be crystallised in accordance with present invention.Amino acid substitutions may include the use of non-naturally occurringanalogues.

[0120] In relation to amino acid sequences, the term “variant” as usedherein refers to additions, deletions or substitutions of amino acidresidues comprised within the wild-type amino acid sequence or fragmentthereof. Preferably, a variant in relation to the amino acid sequence ofthe crystal of the PDE5 of the present invention could include thedeletion or substitution of the histidine (His/H) residue as shownemboldened and underlined in SEQ ID NO: 1 (HRGVNNSYIQRSEHPLAQLYCHSIME),which sequence is comprised in the protein or polypeptide of PDE5 of thecrystal of the present invention. Replacement of said histidine (H)residue is preferably by way of incorporating one or more amino acidresidues (other than histidine), preferably wherein said amino acidresidues are neutral or non-polar.

[0121] The terms “mutant”, “variant”, “homologue”, “analogue”,“derivative” or “fragment” in relation to the nucleotide sequence codingfor the PDE5 of the crystal of the present invention include anysubstitution of, variation of, modification of, replacement of, deletionof, or addition of, one (or more) nucleotide from (or to) the sequenceproviding the resultant nucleotide sequence codes for, or is capable ofcoding for, a PDE5 which is capable of being crystallised.

[0122] In relation to nucleotide sequences, the term “variant” as usedherein refers to additions, deletions or substitutions of nucleotides ofthe wild-type nucleotide sequence or fragment thereof.

[0123] The term “fragment” as used herein refers to any portion of thePDE5 amino acid sequence as defined in the present invention providedthe resultant PDE5 comprising said PDE5 portion is capable of beingcrystallised. Thus, the term “fragment” also includes PDE5, whichcomprises any portion of SEQ ID NOS: 1, 2, 3, 4, 5, or 6.

[0124] An example of a specific fragment of SEQ ID NO: 6 (full-length“loop-swapped” PDE5 sequence) according to the present invention couldbe SEQ ID NO: 5 (“loop-swapped” PDE5 catalytic domain). Moreover, anexample of a specific fragment of SEQ ID NO: 5 (“loop-swapped” PDE5catalytic domain) according to the present invention could be SEQ ID NO:4 (PDE4 “loop region”; HPGVSNQFLINTNSELALMYNDESVLE).

[0125] The term “analogue” as used herein means a sequence similar tothe amino acid sequence of the PDE5 polypeptide of the crystal of thepresent invention or of any one of SEQ ID NOS: 1, 2, 3, 4, 5 or 6, butwherein non-detrimental (i.e. not detrimental to the PDE5's capabilityof being crystallised) amino acid substitutions or deletions have beenmade.

[0126] The term “derivative” as used herein in relation to the aminoacid sequence of the PDE5 of the crystal of the present invention, or ofany one of SEQ ID NOS: 1, 2, 3, 4, 5 or 6, includes chemicalmodification of PDE5. Illustrative of such modifications would bereplacement of hydrogen by an alkyl, acyl, or amino group.

[0127] The term “heavy atom derivative” as used herein in relation tocrystals refers to a crystal comprising macromolecules in the crystallattice which are modified by the inclusion of a heavy atoms (i.e. ofsignificantly greater atomic mass than the atoms common to organicmacromolecules, e.g. carbon, nitrogen, oxygen, phosphorous, etc.) intotheir structure. This is commonly achieved using ionic compounds such assalts of mercury, platinum, gold or silver which may covalently bond tocertain groups on the macromolecule either during co-crystalisation withthe ionic compound or by soaking the compound into the crystal. Otherprocesses may also be used such as derivitisation with seleno-methionineor with noble gases such as Xenon. The purpose of such heavy atomderivatives of crystals is to provide phasing information for structuresolution.

[0128] As used herein a “deletion” is defined as a change in eithernucleotide or amino acid sequence in which one or more nucleotides oramino acid residues, respectively, are absent.

[0129] As used herein an “insertion” or “addition” is a change in anucleotide or amino acid sequence, which has resulted in the addition ofone or more nucleotides or amino acid residues, respectively, ascompared to the sequences of the naturally occurring PDE5.

[0130] As used herein “substitution” results from the replacement of oneor more nucleotides or amino acids by different nucleotides or aminoacids, respectively.

[0131] Conservative substitutions may be made, for example according tothe Table below. Amino acids in the same block in the second column andpreferably in the same line in the third column may be substituted foreach other: ALIPHATIC Non-polar G A P I L V Polar - uncharged C S T M NQ Polar - charged D E K R AROMATIC H F W Y

[0132] The term “homologue” covers homology specifically with respect toprotein structure, primary secondary, tertiary and quartemary, andcovers any structural PDE5 homologue that is capable of beingcrystallised.

[0133] With respect to homology of the amino acid sequences detailedherein, preferably there is at least 70%, more preferably at least 75%,more preferably at least 80%, yet more preferably at least 85%, evenmore preferably at least 90% homology to SEQ ID NOS: 1, 2, 3, 4, 5 or 6.More preferably there is at least 95%, and most preferably at least 98%,homology to SEQ ID NOS: 1, 2, 3, 4, 5 or 6.

[0134] With respect to homology of the nucleotide sequences coding forthe amino acid sequences detailed herein, preferably there is at least70%, more preferably at least 75%, more preferably at least 80%, yetmore preferably at least 85%, even more preferably at least 90% homologyto the nucleotide sequences which code for SEQ ID NOS: 1, 2, 3, 4, 5 or6. More preferably there is at least 95%, and most preferably at least98%, homology to the nucleotide sequences which code for SEQ ID NOS: 1,2, 3, 4, 5 or 6.

[0135] The term “homologue” with respect to the nucleotide sequence ofthe PDE5 as defined in the present invention and the amino acid sequenceof the PDE5 as defined in the present invention may be synonymous withallelic variations of the sequences.

[0136] In particular, the term “homology” as used herein may be equatedwith the term “identity”. Here, sequence homology with respect to, forexample, the amino acid sequence of PDE5 of the crystal of the presentinvention can be determined by a strict comparison of any one or more ofthe sequences with another sequence to see if that other sequence has atleast 70% identity to the sequence(s). Relative sequence homology (i.e.sequence identity) can also be determined by commercially availablecomputer programs that can calculate percentage (%) homology between twoor more sequences. A typical example of such a computer program isCLUSTAL.

[0137] Percentage homology may be calculated over contiguous sequences,i.e. one sequence is aligned with the other sequence and each amino acidin one sequence directly compared with the corresponding amino acid inthe other sequence, one residue at a time. This is called an “ungapped”alignment. Typically, such ungapped alignments are performed only over arelatively short number of residues (for example less than 50 contiguousamino acids).

[0138] Although this is a very simple and consistent method, it fails totake into consideration that, for example, in an otherwise identicalpair of sequences, one insertion or deletion will cause the followingamino acid residues to be put out of alignment, thus potentiallyresulting in a large reduction in % homology when a global alignment isperformed. Consequently, most sequence comparison methods are designedto produce optimal alignments that take into consideration possibleinsertions and deletions without penalising unduly the overall homologyscore. This is achieved by inserting “gaps” in the sequence alignment totry to maximise local homology.

[0139] However, these more complex methods assign “gap penalties” toeach gap that occurs in the alignment so that, for the same number ofidentical amino acids, a sequence alignment with as few gaps aspossible—reflecting higher relatedness between the two comparedsequences—will achieve a higher score than one with many gaps. “Affinegap costs” are typically used that charge a relatively high cost for theexistence of a gap and a smaller penalty for each subsequent residue inthe gap. This is the most commonly used gap scoring system. High gappenalties will of course produce optimised alignments with fewer gaps.Most alignment programs allow the gap penalties to be modified. However,it is preferred to use the default values when using such software forsequence comparisons. For example when using the GCG Wisconsin Bestfitpackage (see below) the default gap penalty for amino acid sequences is−12 for a gap and −4 for each extension.

[0140] Calculation of maximum percentage homology therefore firstlyrequires the production of an optimal alignment, taking intoconsideration gap penalties. A suitable computer program for carryingout such an alignment is the GCG Wisconsin Bestfit package (Universityof Wisconsin, U.S.A.; Devereux et al., 1984, Nucleic Acids Research12:387). Examples of other software than can perform sequencecomparisons include, but are not limited to, the BLAST package (seeAusubel et al., 1999 ibid—Chapter 18), FASTA (Atschul et al., 1990, J.Mol. Biol., 403-410) and the GENEWORKS suite of comparison tools. BothBLAST and FASTA are available for off-line and on-line searching (seeAusubel et al., 1999 ibid, pages 7-58 to 7-60). However, for someapplications it is preferred to use the GCG Bestfit program.

[0141] Although the final percentage homology can be measured in termsof identity, in some cases, the alignment process itself is typicallynot based on an all-or-nothing pair comparison. Instead, a scaledsimilarity score matrix is generally used that assigns scores to eachpairwise comparison based on chemical similarity or evolutionarydistance. An example of such a matrix commonly used is the BLOSUM62matrix—the default matrix for the BLAST suite of programs. GCG Wisconsinprograms generally use either the public default values or a customsymbol comparison table if supplied (see user manual for furtherdetails). It is preferred to use the public default values for the GCGpackage, or in the case of other software, the default matrix, such asBLOSUM62.

[0142] Once the software has produced an optimal alignment, it ispossible to calculate percentage homology, preferably percentagesequence identity. The software typically does this as part of thesequence comparison and generates a numerical result.

[0143] As indicated, for some applications, sequence homology (oridentity) may be determined using any suitable homology algorithm, usingfor example default parameters. For a discussion of basic issues insimilarity searching of sequence databases, see Altschul et al. (1994)Nature Genetics 6:119-129. For some applications, the BLAST algorithm isemployed, with parameters set to default values. The BLAST algorithm isdescribed in detail at http://www.ncbi.nih.gov/BLAST/blast_help.html.Advantageously, “substantial homology” when assessed by BLAST equates tosequences which match with an EXPECT value of at least about 7,preferably at least about 9 and most preferably 10 or more. The defaultthreshold for EXPECT in BLAST searching is usually 10.

[0144] Other computer program methods to determine identify andsimilarity between the two sequences include but are not limited to theGCG program package (Devereux et al. 1984 Nucleic Acids Research 12:387) and FASTA (Atschul et al. 1990 J Molec Biol 403-410).

[0145] The amino acid sequence of the PDE5 of the present inventionpresent invention may be produced by expression of a nucleotide sequencecoding for the same in a suitable expression system.

[0146] In addition, or in the alternative, the protein itself could beproduced using chemical methods to synthesize a PDE5 amino acidsequence, in whole or in part. For example, peptides can be synthesizedby solid phase techniques, cleaved from the resin, and purified bypreparative high performance liquid chromatography (e.g. Creighton(1983) Proteins Structures and Molecular Principles, W H Freeman andCo., New York, N.Y., USA). The composition of the synthetic peptides maybe confirmed by amino acid analysis or sequencing (e.g. the Edmandegradation procedure).

[0147] Direct peptide synthesis can be performed using varioussolid-phase techniques (Roberge J Y et al, Science, Vol 269, 1995, pp.202-204) and automated synthesis may be achieved, for example, using theABI 431 A Peptide Synthesizer (Perkin Elmer, Boston, Mass., USA) inaccordance with the instructions provided by the manufacturer.Additionally, the amino acid sequence of PDE5, or any part thereof, maybe altered during direct synthesis and/or combined using chemicalmethods with a sequence from other subunits, or any part thereof, toproduce a variant polypeptide.

Protein Engineering of PDE5*′

[0148] Analysis of the catalytic domain of wild-type PDE5 protein bymass spectrometry and SDS-PAGE (data not shown) shows that the proteinis cleaved within the region of residues 664-682. High concentrations ofprotease inhibitors provide some stabilisation of the protein, butcleavage still prevents reproducible crystallisation.

[0149] An engineered form of the catalytic domain of PDE5, calledPDE5*′, has been produced where the 657-682 region of PDE5 has beenreplaced by the same region in PDE4 producing a chimeric construct, (seeFIG. 1 for sequence alignment of this region). The C-terminus of thisconstruct is also truncated (C-term 858) compared to the wild-typestructure (C-term 875). Hereafter this engineered construct will bereferred to as PDE5*′.

[0150] This engineered protein has been shown to be stable todegradation by mass spectrometry and SDS-PAGE (data not shown). Theprotein shows improved biophysical properties allowing an alternativepurification protocol to be developed. The new protocol utilises bindingto a Blue sepharose column and specific elution with cGMP. The wild-typeprotein had been shown not to bind to this column probably due to thedisorder of the structure around the protease cleavage site. This PDE5*protein was used to produce crystals with inhibitors which diffract tohigher resolution and have no disordered regions. The protein has alsobeen used reproducibly to produce crystals with further inhibitors whichroutinely diffract to 1.8 Å resolution or higher, making it an improvedprotein for use in structure based drug design.

The Structure of PDE4 and Wild Type PDE5 Catalytic Domains

[0151] (This is also detailed in Application Number PCT/IB02/04426, page28, line 19 to page 29, line 17 and is incorporated herein byreference.)

[0152] The structure of the catalytic domain of PDE4b was published (Xuet al. 2000). A topological comparison of the PDE5 catalytic domain withthe structures in the Protein Data Bank (PDB) does not revealsignificant additional homology with other known protein structuresexcept for the PDE4 structure. Comparisons between the two structureshave been made (FIG. 1 of the present application shows a sequence andsecondary structural alignment of the two proteins). The structure anddomain arrangement is virtually identical to that of PDE4, save that thesecond sub-domain highlighted in PDE4 is only partially present in thePDE5 structure, as detailed below.

[0153] The structure is composed of a single domain of 15 α helicesarranged in a compact fold (FIG. 2 of the present application). Withinthe overall domain, three sub-domains can also be defined. Helices 1 (H1539-545) and 2 (H2 551-554) lie on the exterior of the protein andcomprise the N-terminal region of the construct. These two helices donot overlay with the equivalent ones (H0, H1 and H2) in the PDE4structure. This region is not well conserved across the PDE proteinfamily. Helices 3 (H3 568-582), 4 (H4 584-588), 5 (H5 592-604), 6 (H6615-631) and 7 (H7 640-652) form the first sub-domain of the protein andare contained within the core of the protein. There is no observableelectron density for helices 8 and 9 based on the PDE4 nomenclature.Helix 10 (H10 684-694) is again on the exterior and forms the dimerinterface within the structure. Helices 10 and 11 (H11 706-721) are thevisible portion of the second sub-domain. Helices 12 (H12a 725-731, H12b733-741), 13 (H13 749-765), 14 (H14 772-797), 15 (H15 813-824), 16 (H16826-836) and 17 (H17 841-861) form the third sub-domain of the protein.It should be noted that in PDE5 helix H12 is not a contiguous helix asin PDE4 but is composed of two short helices with a kink in the middleand helix H15 is a contiguous helix in PDE5 but not in PDE4.

Structure of PDE5* Catalytic Domain Complexed with UK-088,800

[0154] The structure of the catalytic domain of PDE5* protein complexedwith UK-088,800 was determined by molecular replacement using onemolecule of the protein structure from the PDE5* complex with Sildenafil(as described in Application Number PCT/IB02/04426: Example 11,“crystallisation of PDE5* with Sildenafil”, page 46, lines 8 to 25;Example 15, “data collection, structure determination and refinementPDE5* with Sildenafil”, page 50, line 9 to page 51, line 6 and Table 6,“atomic co-ordinates for baculovirus-expressed PDE5* complex withSildenafil”, pages 328 to 408; incorporated herein by reference) as abasis for the search model, the co-ordinates for which are included inTable 3 of the present application. The PDE5* catalytic domaincrystallises in the space group C2 as a monomer with one moleculepresent in the asymmetric unit. The C2 form of the PDE5* catalyticdomain crystallises in the space group C2 with approximate celldimensions a=55.97 Å, b=76.55 Å, c=80.50 Å and β=103.09. They containone molecule per asymmetric unit and have a solvent content of 44%(Matthews, 1969). The structure of the PDE5* comprises 17 α helices andthe overall fold is very similar to the wild-type structure with anumber of important differences. The major difference in the structureis the presence of helices H8 and H9 composed of the swapped portionfrom PDE4, residues 657-682. These fold in an identical way to thatobserved in the PDE4 structure and complete the second sub-domain of theprotein. The entire C-terminal region of this construct can also bebuilt into the electron density leaving just three disordered residuesat the N-terminus of this structure. This is likely to contribute to itsenhanced properties for crystallisation.

PDE5*: Active Site and Protein-Inhibitor Interactions

[0155] UK-088,800 occupies the same region of the active site asobserved for the previously described UK-092,480, Sildenafil, asdetailed below (Application Number PCT/IB02/04426: FIG. 4, “A view ofcompound Sildenafil bound to loop swapped PDE5 (PDE5*), page 425;incorporated herein by reference) and demonstrates the same mainlyhydrophobic interactions with the protein (FIG. 3 “Comparison of thefo-fc electron density map contoured at 2.5σ of apo PDE5* (left) andPDE5* soaked with UK-088,800 (right), at the active site region” of thepresent application). The same two direct hydrogen bonds observed in thecomplex of PDE5* with Sildenafil are also observed between Gln 817 ofthe protein and inhibitor (Oε1-N4 2.9 Å and Nε2-O1 3.1 Å).

[0156] Carbon atom C7 of the inhibitor points into a small hydrophobicpocket formed by Leu 765, Ala 767 and Ile 768. These residues, togetherwith Phe 820, form a planar face to the binding site against which thepurine ring of the inhibitor stacks. The opposite side of the purinepacks against Val 782. The C10 propyl substituent form good van derWaals contacts with Phe 786. Phe 786 packs against Leu 804 which in turnforms additional hydrophobic interactions with the phenyl moiety of theinhibitor. The O-alkyl moiety occupies a small pocket bounded by Ala779, Phe 786, Ala 783, Val 782, Leu 804, Ile 813, Met 816 and Gln 817.There is no direct interaction between the inhibitor and the zinc ionfound in the active site. The structure confirms the competitive natureof the mode of inhibition of UK-088,800 by binding in the active site,therefore blocking access for the cGMP substrate (which has also beenmodelled—data not included).

[0157] The main difference comparing Sildenafil and UK-088,800 is thatthe latter inhibitor lacks the sulphonylpiperazine present in Sildenafilwhich points out of the active site.

Wild-Type PDE5-Sildenafil Complex: Active Site and Protein-InhibitorInteractions

[0158] (This is detailed in Application Number PCT/EB02/04426, page 30,line 8 to page 31, line 1, and is incorporated herein by reference.)

[0159] The active site lies mainly within the third sub-domain of theprotein and is bounded by helices H15, H14, the C-terminus of H13, andthe C-terminus of H11, along with the loop region between H11and H12a.The majority of the interactions between the inhibitor and the proteinare hydrophobic in nature, with only two direct hydrogen bonds observed(Application Number PCT/IB02/04426: FIG. 3, page 424, incorporatedherein by reference). The first is between N17 of the purine ring of theinhibitor and Oε1 of Gln 817 (2.8 Å) and the second is from the adjacentoxygen atom O16 of the inhibitor to Nε2 of the same residue Gln 817 (3.1Å).

[0160] Carbon atom C12 of the inhibitor points into a small hydrophobicpocket formed by Leu 765, Ala 767 and Ile 768. These residues, togetherwith Phe 820, form a planar face to the binding site against which thepurine ring of the inhibitor stacks. The opposite side of the purinepacks against Val 782. The C5 propyl substituent forms good van derWaals contacts with Val 782 and Phe 786 and Tyr 612. Phe 786 and Leu 804form additional hydrophobic interactions with the phenyl moiety of theinhibitor. The O-alkyl moiety occupies a small pocket bounded by Ala779, Phe 786, Ala 783, Val 782, Leu 804, Ile 813, Met 816 and Gln 817.The sulphonamide group points out towards the solvent whilst thepiperazine ring is bounded by the extended residues 662-665, althoughwhether the conformation of this part of the structure is unaffected bythe chain break is questionable. There is no direct interaction betweenthe inhibitor and the zinc ion found in the active site. The structureconfirms the competitive nature of the mode of inhibition of Sildenafilby binding in the active site therefore blocking access for the cGMPsubstrate (which has also been modelled - data not included).

Wild Type PDE5-Sildenafil Complex: Metal Ions in the Active Site

[0161] Only one zinc atom is present in the active site of thisstructure. The co-ordination of the ion within the active site is alsoconsistent with that expected for zinc. The metal is co-ordinated by His653 (Nε2-Zn 2.0 Å), His 617 (Nε2-Zn 2.1 Å), Asp 764 (OD2-Zn 2.2 Å) andalso Asp 654 (OD2-Zn 2.2 Å). These residues are completely conservedacross the PDE gene family. There is no evidence of a second metal ionin the active site.

[0162] The present invention will now be described, by way of exampleonly, with reference to the accompanying Sequence Listing and Figures,in which:

[0163] SEQ ID NO: 1 shows the amino acid sequence of the loop regionfrom PDE5.

[0164] SEQ ID NO: 2 shows the amino acid sequence of the wild-type PDE5catalytic domain.

[0165] SEQ ID NO: 3 shows the amino acid sequence of the full-lengthwild-type PDE5 sequence.

[0166] SEQ ID NO: 4 shows the amino acid sequence of the loop region ofPDE4.

[0167] SEQ ID NO: 5 shows the amino acid sequence of the loop-swappedPDE5 catalytic domain=PDE5*.

[0168] SEQ ID NO: 6 shows the amino acid sequence of full-length PDE5sequence comprising PDE5*.

[0169] SEQ ID NOS: 7-14 are oligonucleotide primers.

[0170]FIG. 1 shows an alignment of PDE5 (upper sequence) and PDE4b(lower sequence) catalytic domains. Positions and numbering of helicesfrom the structures are marked for each. Residues in bold show asequence alignment for the engineered region. The sequence from PDE4 hasbeen used to replace the corresponding region in PDE5. This results in aresidue insertion in this region. Underlining highlight C-terminalregion absent in PDE5*.

[0171]FIG. 2 shows a ribbon representation of the overall fold ofproteins showing secondary structure elements. The inhibitor is shown inan all atom stick representation and the metal ions as spheres.(A)=PDE4b, (B)=wild-type PDE5+Sildenafil, (C)=“loop-swapped” PDE5(PDE5*)+Sildenafil. Helices are numbered using PDE4 structure asreference. Helices H0-H7 form sub-domain 1, helices H8-H11 formsub-domain 2, and helices H12-H16 form sub-domain 3.

[0172]FIG. 3: Comparison of the fo-fc electron density map contoured at2.5 σ of apo PDE5* (“loop-swapped” PDE5) (left) and PDE5* soaked withUK-088,800 (right), at the active site region.

[0173]FIG. 4: A two dimensional representation of the structure ofUK-088,800, 5-(2-ethoxyphenyl)-1 -methyl-3-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one (only the Hydrogen on N4is illustrated).

EXPERIMENTAL SECTION EXAMPLE 1 Construction and Expression of PDE5Wild-Type Catalytic Domain (E534-N875)

[0174] Oligonucleotide primers were designed from the sequence of humanPDE5 (Accession number=AB001635). DNA fragments were generated by PCRamplification from a full-length PDE5 clone. The followingoligonucleotides were used: PDE5 5′ Untagged Oligo: (SEQ ID NO:7)CGTGAATTCATGGAGGAAGAAACAAGAGAGCTAC PDE5 3′ Long Oligo: (SEQ ID NO:8)CGTTCTAGACTATCAGTTCCGCTTGGCCTGGCCGCTTTCCCC

[0175] The PCR reaction was carried out for 30 cycles in a total volumeof 50 μl in a solution containing 1.5 mM MgCl₂, 200 μM dNTPs, 50 pmol ofeach primer and 2.5 units of Expand DNA polymerase (Roche, East Sussex,UK). Each cycle was 94° C., 1 min, 50° C., 1 min and 72° C., 2 mins.

[0176] The final amplified DNA fragments for both constructs wereseparated on a 1% agarose gel and purified using a QIAquick gelextraction kit (Qiagen, West Sussex, UK). The fragment was then digestedusing EcoRI and XbaI, and ligated into pFastbac1 EcoRI/XbaI-digestedvector (Life Technologies, Paisley, UK). The ligation was carried out at12° C. for 16 hours. The ligation mix was then electroporated into E.coli (TOP 10) (Invitrogen, Gronigen, The Netherlands).

[0177] Clones containing the desired insert were selected by using 2YTplates containing 100 μg/ml ampicillin and checked using endonucleasedigestion for presence of correct size insert. DNA sequence analysis wascarried out by Lark (Saffron Waldon, UK).

[0178] Recombinant bacmid DNA was produced by transforming E.coliDH10BAC™ with pFastbac1::PDE5 catalytic domain (534-875) plasmid DNA.This was carried out according to the method shown in the Bac to Bac™baculovirus expression manual (Life Technologies, Paisley, UK). PCRanalysis was used to verify successful transposition to the bacmid usingpUC/M13 amplification primers (Invitrogen, Gronigen, The Netherlands).

[0179] Generation of primary baculovirus stocks was carried out bytransfection using Sf-9 insect cells. Bacmid DNA containing the correctinsert was mixed with CELLFECTIN™ transfection reagent (LifeTechnologies, Paisley, UK) and added to a monolayer of Sf-9 insect cellsusing SF-900II serum free medium (Invitrogen, Gronigen, TheNetherlands). Following 72 hours incubation at 27° C. the supernatantwas harvested as the initial baculovirus stock. This stock was amplifiedby adding the initial virus stock into a suspension of Sf-9 insect cellsat 1×10⁶ cells/ml in 1 litre Erlenmeyer flasks (Coming Life Sciences,New York, USA), at an agitation of 125 rpm at 27° C. After 6 days postinfection the supernatant was harvested by centrifugation and stored at4° C. as the working virus stock. The titre of this working stock wasdetermined by conventional plaque assay analysis as in the Bac to Bacbaculovirus expression manual (Invitrogen, Gronigen, The Netherlands).

[0180] Protein expression was optimised in Erlenmeyer flask culturesusing Sf-9 and T.ni High5 insect cell cultures looking at differentmultiplicity's of infection (MOI) and harvest times, the optimalconditions found were then scaled up into fermenters.

[0181] The fermenters used were autoclavable Applikon 3 litre stirredvessels controlled using Applikon 1030 biocontrollers. Inoculum of T.niHigh5 cells was initially prepared from shake flask cultures. Thefermenter was inoculated with 5×10⁵ cells/ml, with an initial workingvolume of 1.8 litres made up in Excel 405 serum free medium (JRHBiosciences, Kansas, USA). Temperature was controlled at 27° C.,dissolved oxygen concentration controlled at 60% and pH was measured butnot controlled. Oxygen concentration was controlled throughout.Agitation was set at 150 rpm with a double impeller system of marineimpeller within the culture and Rushton impeller at the liquid/headspaceinterface. Aeration was continuous to the headspace at 0.5 l/min.

[0182] When the viable cell density reached 2×10⁶ cells/ml the culturewas infected using an MOI of 1 from the titred baculovirus workingstock. Harvest time for the culture was 48 hours post infection. Thiswas achieved by centrifugation at 2000 g for 15 mins; the insect cellpellet was then stored at −80° C. prior to purification.

EXAMPLE 2 Construction and Expression of His6-Tagged PDE5 Wild-TypeCatalytic Domain (E534-N875)

[0183] Oligonucleotide primers were designed from the sequence of humanPDE5 (=PDE5A1 isoform; Accession number=AB001635). DNA fragments weregenerated by PCR amplification from a full-length PDE5 clone. Thefollowing oligonucleotides were used: PDE5 5′ His6 OligoCGTGAATTCATGCATCATCATCATCATCATCTTCTGGTTCCGCGTGGATCTG (SEQ ID NO:9)CGCCCGAGGAAGAAACAAGAGAGCTAC PDE5 3′ Long OligoCGTTCTAGACTATCAGTTCCGCTTGGCCTGGCCGCTTTCCCC (SEQ ID NO:8)

[0184] The PCR reaction was carried out for 30 cycles in a total volumeof 50 μl in a solution containing 1.5 nM MgCl₂, 200 μM dNTPs, 50 pmol ofeach primer and 2.5 units of Expand DNA polymerase (Roche, East Sussex,UK). Each cycle was 94° C., 1 min, 50° C., 1 min and 72° C., 2 mins.

[0185] The final amplified DNA fragments for both constructs wereseparated on a 1% agarose gel and purified using a QIAquick gelextraction kit (Qiagen, West Sussex, UK). The fragment was then digestedusing EcoRI and XbaI, and ligated into pFastbac1 EcoRI/XbaI-digestedvector (Life Technologies, Paisley, UK). The ligation was carried out at12° C. for 16 hours. The ligation mix was then electroporated into E.Coli (TOP 10) (Invitrogen, Gronigen, The Netherlands).

[0186] Clones containing the desired insert were selected by using 2YTplates containing 100 μg/ml ampicillin and checked using endonucleasedigestion for presence of correct size insert. DNA sequence analysis wascarried out by Lark (Saffron Waldon, UK).

[0187] Methods to generate the recombinant baculovirus were as those forwild-type PDE5 catalytic domain (see EXAMPLE 1).

[0188] Expression optimisation again showed T.ni High5 insect cells togive the best expression. Therefore baculovirus expression in fermenterswas carried out using the same procedures as for the previous construct.

EXAMPLE 3 Construction and Expression of PDE5* (E534-E858) inBaculovirus

[0189] The PDE5* construct was produced by using overlap extension PCRwhere the following oligonucleotides were used: A:CGTGAATTCATGGAGGAAGAAACAAGAGAGCTAC (SEQ ID NO:7) B:CAAAGAAAGTTCTGAATTTGTGTTGATGAGAAACTGATTGGAGACTCCA (SEQ ID NO:10)GGATGATCCAAATCGTGGCTTAG C:ATCAACACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTT (SEQ ID NO:11)GGAACACCATCATTTTGACCAG D: CGTTCTAGACTATCATTCTGCAAGGGCCTGCCATTTCTG (SEQID NO:12)

[0190] Initial DNA fragments were generated using oligonucleotides A+Band C+D with the same template DNA as for the wild-type PDE5 catalyticdomain construct. The PCR reaction was carried out for 30 cycles in atotal volume of 50 μl in a solution containing 1.5 mM MgCl₂, 200 μMdNTPs, 50 pmol of each primer and 2 units of Expand DNA polymerase(Roche, East Sussex, UK). Each cycle was 94° C., 1 min, 50° C., 2 min,and 72° C., 3 min. In the second round of PCR, DNA products from PCR A+Band C+D were used as template DNA with the oligonucleotides A+D used toamplify the full-length construct. The PCR conditions were the same asthe initial PCR reaction. This generates a construct with the PDE4swapped region and a C-terminal truncation (C-term 858) as compared toPDE5 catalytic domain (C-term 875).

[0191] Methods to generate the recombinant baculovirus were as those forwild-type PDE5 catalytic domain (see EXAMPLE 1).

[0192] Expression optimisation again showed T.ni High5 insect cells togive the best expression. Therefore baculovirus expression in fermenterswas carried out using the same procedures as for the previous construct.

EXAMPLE 4 Construction and Expression of PDE5* (E534-E858) in E. coli

[0193] The PDE5* construct in E. coli was produced by using PCR wherethe following oligonucleotides were used and the template DNA beingpFastbac1::PDE5* plasmid DNA (sequence verified), produced in EXAMPLE 3.(SEQ ID NO:13) E: CGTCATATGGAGGAAGAAACAAGAGAGCTAC (SEQ ID NO:14) F:CGTCTCGAGCTATCATTCTGCAAGGGCCTGCCATTTCTG

[0194] The PCR reaction was carried out for 30 cycles in a total volumeof 50 μl in a solution containing 1.5 mM MgCl₂, 200 μM dNTPs, 50 pmol ofeach primer and 2.5 units of Expand DNA polymerase (Roche, East Sussex,UK). Each cycle was 94° C., 1 min, 50° C., 1 min and 72° C., 2 mins.

[0195] The final amplified DNA fragment was separated on a 1% agarosegel and purified using a QIAquick gel extraction kit (Qiagen, WestSussex, UK). The fragments were then digested using Nde1 and Xho1, andligated into pET21C (Novagen, Nottingham, UK) Nde1/Xho1-digested vector.The ligation was carried out at 12° C. for 16 hours. The ligation mixwas then electroporated into E. coli (TOP 10) (Invitrogen, Gronigen, TheNetherlands).

[0196] Clones containing the desired insert were selected by using 2YTplates containing 100 μg/ml ampicillin. Plasmid DNA was also checkedusing endonuclease digestion for presence of correct size insert. DNAsequence analysis was carried out by Lark (Saffron Waldon, UK).

[0197] The correctly sequenced plasmid DNA was then electroporated intoE. coli BL21 (DE3) (Novagen, Nottingham, UK) for expression. Expressionwas carried out in 7 litre Applikon fermenters using 5 litre 2YT brothcontaining 100μg/ml carbenicillin as the medium. Agitation was set at1000 rpm using a double rushton impeller assembly and aeration to thesparger at 2 litres/min. The fermenter was inoculated with an overnightshake flask culture grown at 37° C. and 200 rpm, the inoculation densitywas 1 % vol/vol. The fermentation was pH controlled at 7.2 using 20%vol/vol NH₄OH solution and temperature initially set to 37° C. When theOD_(600 nm) reached 1.5 the temperature set-point was reduced to 25° C.and then the culture was induced with IPTG at a final concentration of 1mM. The fermentation was then harvested 4 hours post-induction by batchcentrifugation (8,000 rpm for 10 minutes). The final pellet was thenfrozen (−80° C.) to await subsequent purification.

EXAMPLE 5 Purification of PDE5* Catalytic Domain

[0198] Pellet from the E. coli fermentation was resuspended into 10 mlslysis buffer per gram wet cell weight and mechanically broken using acontinuous cell disrupter (Constant Systems, Warwickshire, UK) at apressure of 20 kpsi. The lysis buffer consisted of 50 mM Tris HCl (pH7.5), 100 mM NaCl, 1 mM DTT containing EDTA-free protease inhibitorcocktail tablets (Roche, East Sussex, UK) and 10 μM E-64. The lysate waschilled and centrifuged at 14000 g for 45 min to remove cell debris. Allpurifications were subsequently carried out using an Äkta Explorerpurification system (Amersham Pharmacia, Buckinghamshire, UK). Thesupernatant was applied to a 50 ml Q—sepharose fast-flow column(Amersham Pharmacia, Buckinghamshire, UK) at 5 ml/min with theflow-through collected. The flow-through sample was then applied at 50ml/min to a 2 litre G-25 superfine desalting column (Amersham Pharmacia,Buckinghamshire, UK) pre-equilibrated in Blue sepharose buffer A (50 mMBis-Tris (pH 6.4), 50 mM NaCl, 2 mM EDTA, 2 mM EGTA and 1 mM DTT). Theprotein fraction was eluted in Blue sepharose buffer A.

[0199] The next column step was carried out in series, loading thesample initially onto a 20 ml SP-sepharose high performance column(Amersham Pharmacia, Buckinghamshire, UK) then flow-through from thisdirectly onto a 10 ml Blue sepharose fast-flow column (AmershamPharmacia, Buckinghamshire, UK) at a flow-rate of 2 ml/min. Once loadingwas complete, the SP-sepharose column was taken out of line and the Bluesepharose column washed with 5 column volumes of Blue sepharose bufferA. The column was washed with Blue sepharose buffer A containing 1 MNaCl until the absorbance 280 nm reached baseline and then washed with 5column volumes of Blue sepharose buffer A. PDE5* protein was step-elutedusing Blue sepharose buffer containing 20 mM cGMP (Na-salt) (Sigma,Dorset, UK). Fractions were assayed on Tris-glycine SDS gels(Invitrogen, Gronigen, The Netherlands) and pooled accordingly. Thesefractions were concentrated to 2.5 mg/ml using centrifugal concentrators(Vivascience, Gloucestershire, UK) and loaded at 1.5 ml/min onto aSuperdex-200 prep grade {fraction (26/60)} column pre-equilibrated with50 mM Bis-Tris (pH 6.8), 500 mM NaCl, 1 mM DTT and 2 μM E-64. The elutedfractions were analysed on Tris-glycine SDS PAGE gels.

EXAMPLE 6 Crystallisation of PDE5*

[0200] The PDE5* fractions from the final gel filtration column werepooled (total volume of 25 mls) and the protein concentration wasassayed (0.2 mg/ml). The protein solution was supplemented with 10 μME-64 and 1 mg/ml leupeptin (Sigma, Dorset, UK). The solution wasconcentrated to 10 mg/ml using a Centriprep 10 kDa Molecular weightcut-off centrifugal concentrator (Amicon Bioseparations, Maine, USA) at3,000rpm, 4° C. Prior to crystallisation, the protein solution wascentrifuged for 5 min at 14,000 rpm in an Eppendorf centrifuge.

[0201] Hanging drop vapour diffusion crystallisation trials were set upat 4° C. Drops comprised of 2 μl reservoir buffer mixed with 2 μlprotein solution were suspended on cover slips over 500 μl reservoirsolutions containing 0.1M sodium HEPES pH 7.4, 20% Polyethylene glycol4000 and 10% iso-Propanol. Plate-shaped crystals, up to 700 μm inlargest dimension, grew after 1-3 days. Crystals were transferred to a20 μl drop of 0.1 M sodium HEPES pH 7.4 and 20% Polyethylene glycol 4000in square microbridges. Crystals were then transferred to a solution of0.1 M sodium HEPES pH 7.4, 20% Polyethylene glycol 4000 with 15%glycerol and then frozen during X-ray data collection.

[0202] The crystals belong to space group C2 with cell dimensionsa=55.97 Å, b=76.55 Å, c=80.50 Å and β=103.09. They contain one moleculeper asymmetric unit and have a solvent content of 44% (Matthews, 1969).

EXAMPLE 7 Soaking Inhibitor into PDE5*

[0203] Plate-shaped crystals of apo PDE5* obtained according to methodsdetailed in EXAMPLE 6 were transferred to a 20 μ;l drop of 0.1M sodiumHEPES and 20% Polyethylene glycol 4000 in square microbridges. To this,1.0 μl of a 20 mg/ml concentration of inhibitor dissolved in DMSO wasadded. Crystals were then transferred to a solution of 0.1M sodium HEPESpH 7.4, 20% Polyethylene glycol 4000 with 15% glycerol and then frozenduring X-ray data collection.

EXAMPLE 8 Data Collection, Structure Determination and Refinement of theSoakable C2 Crystal form of PDE5*

[0204] The structure of the E. coli-engineered PDE5* was solved bymolecular replacement (MR) using the coordinates of one subunit of PDE5*in the P2₁ crystal form (the crystals belong to the monoclinic spacegroup P2₁ with unit cell dimensions a=54.93 Å, b=77.77 Å, c=82.05 Å,α=γ90° β100.9550°) the coordinate set is detailed in Table 3. Molecularreplacement was performed using AMORE (CCP4, J.Navaza 1994). Theresulting map was of good quality and the structure was refitted usingQUANTA® (Accelrys products).

[0205] A representative X-ray diffraction data set was collected with aRigaku Satum92 CCD detector on an in-house FR-D rotating anode (Rigaku),with Osmic mirrors (MSC). Data were processed using theCrystalClear/D*Trek processing package (Rigaku-MSC). Data collectionstatistics are summarised in Table 1 (Apo).

[0206] The crystals belong to space group C2 with cell dimensionsa=55.97 Å, b=76.55 Å, c=80.50 Å and β=103.09. They contain one moleculeper asymmetric unit and have a solvent content of 44% (Matthews, 1968).

[0207] Refinement was carried out in the resolution range 30-1.6 Å usingCNX (Brüinger et al., 1998) with the “mlf” maximum likelihood targetfunction. Partial structure factors from a flat bulk-solvent model andanisotropic B-factor correction were supplied throughout the refinement.The R-factor for the refined model is 0.231 (free R-factor, 5% of data,0.267) for all data in the resolution range 30-1.6 Å. The refinementstatistics are summarised in Table 2 (Apo).

[0208] The co-ordinate set for the refined model of apo PDE5* isrecorded in Table 4. The model contains 323 amino acid residues, 537-858(residue Glu 681A has been numbered to maintain PDE5 numbering scheme),a zinc ion and a magnesium ion, as well as 222 water molecules.

EXAMPLE 9 Data Collection, Structure Determination and Refinement of theSoakable C2 Crystal form of PDE5* Soaked with UK-088,800

[0209] The structure of the UK-088,800 soaked into the C2 crystal formof PDE5* was solved by difference Fourier methods.

[0210] X-ray diffraction data were collected with an RaxisIV image platedetector on an in-house FR-D rotating anode (Rigaku), with Osmic mirrors(MSC). All data were processed using the HKL package (Otwinowski &Minor, 1997). Data collection statistics are summarised in Table 1(UK-088,800).

[0211] Refinement was carried out in the resolution range 30-1.5 Å usingCNX (Brüinger et al., 1998) with the “mlf” maximum likelihood targetfunction. Partial structure factors from a flat bulk-solvent model andanisotropic B-factor correction were supplied throughout the refinement.The R-factor for the refined model is 0.219 (free R-factor, 5% of data,0.228) for all data in the resolution range 30-1.5 Å. The refinementstatistics are summarised in Table 2 (UK-088,800).

[0212] The co-ordinate set for the refined model of PDE5*-UK-088,800 isrecorded in Table 5. The model contains 323 amino acid residues, 537-858(residue Glu 681A has been numbered to maintain PDE5 numbering scheme),the ligand UK-088,800, a zinc ion and a magnesium ion, as well as 183water molecules.

EXAMPLE 10 Comparison of the apo PDE5* and PDE5* Soaked with UK-088,800

[0213] The (fo-fc)α_(calc) electron density map of PDE5* soaked withUK-088,800 calculated with experimental structure factor amplitudes andmodel phases derived prior to incorporation of the ligand into themodel, shows a clearly featured peak that can unequivocally beinterpreted as UK-088,880 (FIG. 3). In contrast, the equivalent(fo-FC)α_(calc) electron density map of apo PDE5* shows no significantresidual features that could be interpreted as a small molecule ligand.The experiment allowed the experimental determination of the bindingmode of UK-088,800 to PDE5* and demonstrates that the C2 crystal form ofPDE5* as described herein is amenable to ligand soaking. The structureof PDE5* in the C2 crystal form does not show significant differences tothat observed with the P2₁ crystal form. TABLE 1 Data collectionstatistics for the soakable C2 crystal form of PDE5* Apo UK-088,800Resolution [Å] 1.6 1.5 Unique reflections 41189 52038 Completeness [%]94.5 99.5 Redundancy 2.9 3.5 R_(sym) ^(a) 0.074 0.049$\quad^{a}R_{sym} = {\sum\limits_{hkl}{\sum\limits_{i}{{{{I_{i}({hkl})} - \overset{\_}{I({hkl})}}}/{\sum\limits_{hkl}{\sum\limits_{i}{{I_{i}({hkl})}}}}}}}$

[0214] TABLE 2 Refinement statistics of soakable C2 crystal form ofPDE5* Apo UK-088,800 Resolution range, Å 30.0-1.6 30.0-1.5 Amino acidresidues, no. 323 323 Water molecules, no. 222 183 rmsd bond length, Å0.005 0.005 rmsd bond angles, ° 1.130 1.158 ^(a)R-factor 0.231 0.219Free R-factor (5 % of data) 0.267 0.228$\quad^{a}R = {{\sum\limits_{hkl}{F_{obs}}} - {k{{F_{calc}}/{\sum\limits_{hkl}{F_{obs}}}}}}$

[0215] TABLE 3 Atomic coordinates for baculovirus-expressed PDE5*complex with Sildenafil Atom Number, Atom Type, Residue Type, ResidueNumber Cartesian Coordinates X, Y, Z, Atom Occupancy (O) and TemperatureFactor (B) X Y Z O B ATOM 1 CB THR A 537 −3.008 28.295 13.745 1.00 40.04ATOM 2 OG1 THR A 537 −4.423 28.364 13.527 1.00 40.20 ATOM 3 CG2 THR A537 −2.273 28.516 12.435 1.00 40.01 ATOM 4 C THR A 537 −2.764 26.99815.853 1.00 42.52 ATOM 5 O THR A 537 −3.657 26.395 16.451 1.00 44.33ATOM 6 N THR A 537 −3.513 25.856 13.760 1.00 44.29 ATOM 7 CA THR A 537−2.652 26.924 14.338 1.00 43.47 ATOM 8 N ARG A 538 −1.857 27.751 16.4661.00 33.65 ATOM 9 CA ARG A 538 −1.818 27.897 17.916 1.00 31.51 ATOM 10CB ARG A 538 −3.201 28.267 18.463 1.00 51.67 ATOM 11 CG ARG A 538 −3.42027.913 19.928 1.00 52.25 ATOM 12 CD ARG A 538 −2.377 28.532 20.845 1.0052.37 ATOM 13 NE ARG A 538 −1.851 27.547 21.788 1.00 52.59 ATOM 14 CZARG A 538 −1.048 27.833 22.809 1.00 52.58 ATOM 15 NH1 ARG A 538 −0.67629.087 23.032 1.00 52.27 ATOM 16 NH2 ARG A 538 −0.608 26.864 23.600 1.0052.33 ATOM 17 C ARG A 538 −1.336 26.584 18.521 1.00 30.67 ATOM 18 O ARGA 538 −0.175 26.465 18.906 1.00 30.03 ATOM 19 N GLU A 539 −2.221 25.59418.593 1.00 27.90 ATOM 20 CA GLU A 539 −1.827 24.310 19.151 1.00 27.13ATOM 21 CB GLU A 539 −3.000 23.322 19.146 1.00 33.40 ATOM 22 CG GLU A539 −2.627 21.946 19.679 1.00 34.46 ATOM 23 CD GLU A 539 −3.814 21.00719.761 1.00 34.35 ATOM 24 OE1 GLU A 539 −4.656 21.037 18.843 1.00 34.50ATOM 25 OE2 GLU A 539 −3.899 20.233 20.738 1.00 34.57 ATOM 26 C GLU A539 −0.666 23.734 18.346 1.00 27.02 ATOM 27 O GLU A 539 0.280 23.18918.909 1.00 27.32 ATOM 28 N LEU A 540 −0.739 23.866 17.027 1.00 26.77ATOM 29 CA LEU A 540 0.320 23.354 16.166 1.00 26.36 ATOM 30 CB LEU A 540−0.070 23.496 14.695 1.00 24.87 ATOM 31 CG LEU A 540 1.027 23.155 13.6821.00 24.86 ATOM 32 CD1 LEU A 540 1.426 21.689 13.833 1.00 25.12 ATOM 33CD2 LEU A 540 0.531 23.447 12.264 1.00 25.63 ATOM 34 C LEU A 540 1.63124.091 16.415 1.00 26.72 ATOM 35 O LEU A 540 2.681 23.479 16.603 1.0026.47 ATOM 36 N GLN A 541 1.573 25.416 16.407 1.00 25.80 ATOM 37 CA GLNA 541 2.777 26.196 16.626 1.00 26.31 ATOM 38 CB GLN A 541 2.455 27.68216.484 1.00 28.46 ATOM 39 CG GLN A 541 2.334 28.108 15.029 1.00 28.55ATOM 40 CD GLN A 541 1.709 29.475 14.868 1.00 28.37 ATOM 41 OE1 GLN A541 1.843 30.334 15.736 1.00 28.46 ATOM 42 NE2 GLN A 541 1.033 29.68713.747 1.00 29.26 ATOM 43 C GLN A 541 3.415 25.894 17.978 1.00 25.96ATOM 44 O GLN A 541 4.636 25.785 18.082 1.00 26.05 ATOM 45 N SER A 5422.589 25.733 19.008 1.00 27.15 ATOM 46 CA SER A 542 3.103 25.440 20.3411.00 27.52 ATOM 47 CB SER A 542 1.980 25.510 21.379 1.00 38.20 ATOM 48OG SER A 542 1.535 26.841 21.558 1.00 38.87 ATOM 49 C SER A 542 3.75224.067 20.390 1.00 27.50 ATOM 50 O SER A 542 4.795 23.888 21.015 1.0027.75 ATOM 51 N LEU A 543 3.131 23.095 19.732 1.00 23.90 ATOM 52 CA LEUA 543 3.676 21.743 19.723 1.00 23.62 ATOM 53 CB LEU A 543 2.702 20.78519.022 1.00 31.43 ATOM 54 CG LEU A 543 2.929 19.274 19.167 1.00 32.27ATOM 55 CD1 LEU A 543 1.959 18.529 18.263 1.00 31.54 ATOM 56 CD2 LEU A543 4.340 18.904 18.800 1.00 32.06 ATOM 57 C LEU A 543 5.025 21.72519.009 1.00 23.65 ATOM 58 O LEU A 543 5.998 21.144 19.498 1.00 23.61ATOM 59 N ALA A 544 5.079 22.365 17.848 1.00 24.41 ATOM 60 CA ALA A 5446.295 22.402 17.052 1.00 24.73 ATOM 61 CB ALA A 544 6.014 23.090 15.7281.00 23.31 ATOM 62 C ALA A 544 7.477 23.076 17.748 1.00 25.97 ATOM 63 OALA A 544 8.619 22.642 17.600 1.00 25.19 ATOM 64 N ALA A 545 7.20224.125 18.512 1.00 29.21 ATOM 65 CA ALA A 545 8.259 24.861 19.196 1.0030.03 ATOM 66 CB ALA A 545 7.837 26.315 19.351 1.00 32.13 ATOM 67 C ALAA 545 8.660 24.288 20.553 1.00 30.21 ATOM 68 O ALA A 545 9.698 24.65721.105 1.00 30.14 ATOM 69 N ALA A 546 7.849 23.382 21.088 1.00 28.91ATOM 70 CA ALA A 546 8.126 22.790 22.391 1.00 28.92 ATOM 71 CB ALA A 5466.878 22.068 22.913 1.00 27.14 ATOM 72 C ALA A 546 9.308 21.831 22.4001.00 29.12 ATOM 73 O ALA A 546 9.648 21.222 21.381 1.00 29.57 ATOM 74 NVAL A 547 9.936 21.702 23.564 1.00 27.29 ATOM 75 CA VAL A 547 11.06020.791 23.714 1.00 26.19 ATOM 76 CB VAL A 547 11.917 21.148 24.947 1.0037.00 ATOM 77 CG1 VAL A 547 12.925 20.042 25.223 1.00 37.18 ATOM 78 CG2VAL A 547 12.635 22.464 24.711 1.00 37.04 ATOM 79 C VAL A 547 10.48219.395 23.903 1.00 26.09 ATOM 80 O VAL A 547 9.473 19.226 24.588 1.0027.35 ATOM 81 N VAL A 548 11.110 18.400 23.286 1.00 28.09 ATOM 82 CA VALA 548 10.638 17.029 23.409 1.00 28.48 ATOM 83 CB VAL A 548 10.792 16.25422.079 1.00 23.53 ATOM 84 CG1 VAL A 548 10.198 14.845 22.215 1.00 24.59ATOM 85 CG2 VAL A 548 10.123 17.016 20.953 1.00 23.63 ATOM 86 C VAL A548 11.468 16.336 24.475 1.00 28.05 ATOM 87 O VAL A 548 12.637 16.03324.252 1.00 29.14 ATOM 88 N PRO A 549 10.879 16.080 25.655 1.00 28.24ATOM 89 CD PRO A 549 9.550 16.472 26.151 1.00 28.37 ATOM 90 CA PRO A 54911.647 15.414 26.709 1.00 28.05 ATOM 91 CB PRO A 549 10.648 15.32127.858 1.00 28.48 ATOM 92 CG PRO A 549 9.781 16.524 27.640 1.00 28.59ATOM 93 C PRO A 549 12.133 14.045 26.254 1.00 28.74 ATOM 94 O PRO A 54911.639 13.495 25.262 1.00 27.64 ATOM 95 N SER A 550 13.103 13.505 26.9771.00 30.38 ATOM 96 CA SER A 550 13.658 12.202 26.649 1.00 30.47 ATOM 97CB SER A 550 14.923 11.963 27.464 1.00 32.70 ATOM 98 OG SER A 550 14.61111.959 28.843 1.00 32.28 ATOM 99 C SER A 550 12.654 11.101 26.955 1.0029.91 ATOM 100 O SER A 550 11.683 11.310 27.684 1.00 30.19 ATOM 101 NALA A 551 12.898 9.922 26.396 1.00 27.46 ATOM 102 CA ALA A 551 12.0228.784 26.626 1.00 27.31 ATOM 103 CB ALA A 551 12.451 7.610 25.756 1.0033.59 ATOM 104 C ALA A 551 12.064 8.389 28.097 1.00 27.99 ATOM 105 O ALAA 551 11.031 8.093 28.700 1.00 27.97 ATOM 106 N GLN A 552 13.264 8.38228.670 1.00 30.15 ATOM 107 CA GLN A 552 13.433 8.019 30.074 1.00 31.28ATOM 108 CB GLN A 552 14.917 8.099 30.457 1.00 50.35 ATOM 109 CG GLN A552 15.547 9.470 30.254 1.00 51.01 ATOM 110 CD GLN A 552 17.068 9.43930.310 1.00 51.35 ATOM 111 OE1 GLN A 552 17.725 8.932 29.398 1.00 51.08ATOM 112 NE2 GLN A 552 17.635 9.979 31.385 1.00 51.12 ATOM 113 C GLN A552 12.595 8.934 30.969 1.00 31.11 ATOM 114 O GLN A 552 11.888 8.47031.868 1.00 30.93 ATOM 115 N THR A 553 12.660 10.232 30.704 1.00 32.81ATOM 116 CA THR A 553 11.904 11.202 31.484 1.00 32.49 ATOM 117 CB THR A553 12.250 12.637 31.060 1.00 35.77 ATOM 118 OG1 THR A 553 13.615 12.91531.399 1.00 35.76 ATOM 119 CG2 THR A 553 11.339 13.639 31.761 1.00 35.80ATOM 120 C THR A 553 10.399 10.999 31.333 1.00 32.89 ATOM 121 O THR A553 9.658 11.065 32.313 1.00 33.04 ATOM 122 N LEU A 554 9.954 10.75030.105 1.00 29.86 ATOM 123 CA LEU A 554 8.534 10.545 29.827 1.00 28.95ATOM 124 CB LEU A 554 8.278 10.693 28.325 1.00 27.17 ATOM 125 CG LEU A554 8.586 12.088 27.769 1.00 27.34 ATOM 126 CD1 LEU A 554 8.439 12.10126.255 1.00 27.36 ATOM 127 CD2 LEU A 554 7.650 13.105 28.410 1.00 27.14ATOM 128 C LEU A 554 8.011 9.197 30.326 1.00 28.80 ATOM 129 O LEU A 5546.803 9.014 30.486 1.00 28.57 ATOM 130 N LYS A 555 8.925 8.260 30.5611.00 24.74 ATOM 131 CA LYS A 555 8.588 6.935 31.071 1.00 25.34 ATOM 132CB LYS A 555 7.764 7.072 32.356 1.00 44.27 ATOM 133 CG LYS A 555 8.4207.960 33.402 1.00 45.10 ATOM 134 CD LYS A 555 7.451 8.363 34.501 1.0045.29 ATOM 135 CE LYS A 555 8.106 9.352 35.455 1.00 45.10 ATOM 136 NZLYS A 555 7.173 9.818 36.518 1.00 45.31 ATOM 137 C LYS A 555 7.818 6.08430.060 1.00 24.58 ATOM 138 O LYS A 555 7.148 5.116 30.433 1.00 25.45ATOM 139 N ILE A 556 7.932 6.430 28.783 1.00 26.12 ATOM 140 CA ILE A 5567.222 5.699 27.740 1.00 26.45 ATOM 141 CB ILE A 556 7.160 6.515 26.4321.00 24.50 ATOM 142 CG2 ILE A 556 6.294 7.753 26.640 1.00 24.65 ATOM 143CG1 ILE A 556 8.571 6.907 25.987 1.00 24.30 ATOM 144 CD1 ILE A 556 8.6317.477 24.582 1.00 24.18 ATOM 145 C ILE A 556 7.806 4.321 27.446 1.0026.74 ATOM 146 O ILE A 556 7.203 3.525 26.722 1.00 26.46 ATOM 147 N THRA 557 8.974 4.027 28.004 1.00 26.58 ATOM 148 CA THR A 557 9.571 2.71827.782 1.00 26.91 ATOM 149 CB THR A 557 11.098 2.750 27.964 1.00 33.52ATOM 150 OG1 THR A 557 11.653 3.811 27.179 1.00 33.53 ATOM 151 CG2 THR A557 11.709 1.430 27.506 1.00 33.78 ATOM 152 C THR A 557 8.983 1.71128.766 1.00 26.91 ATOM 153 O THR A 557 9.108 0.501 28.578 1.00 27.08ATOM 154 N ASP A 558 8.327 2.213 29.810 1.00 22.97 ATOM 155 CA ASP A 5587.739 1.347 30.824 1.00 24.55 ATOM 156 CB ASP A 558 7.564 2.101 32.1451.00 42.16 ATOM 157 CG ASP A 558 8.816 2.834 32.573 1.00 43.08 ATOM 158OD1 ASP A 558 9.918 2.258 32.459 1.00 43.16 ATOM 159 OD2 ASP A 558 8.6923.987 33.036 1.00 43.34 ATOM 160 C ASP A 558 6.386 0.797 30.408 1.0023.87 ATOM 161 O ASP A 558 5.522 1.537 29.940 1.00 24.35 ATOM 162 N PHEA 559 6.200 −0.505 30.593 1.00 26.69 ATOM 163 CA PHE A 559 4.936 −1.14030.257 1.00 26.24 ATOM 164 CB PHE A 559 5.052 −2.662 30.372 1.00 34.04ATOM 165 CG PHE A 559 5.885 −3.290 29.292 1.00 34.73 ATOM 166 CD1 PHE A559 5.537 −3.135 27.952 1.00 34.65 ATOM 167 CD2 PHE A 559 7.018 −4.03629.610 1.00 34.64 ATOM 168 CE1 PHE A 559 6.304 −3.713 26.943 1.00 34.43ATOM 169 CE2 PHE A 559 7.793 −4.618 28.610 1.00 34.92 ATOM 170 CZ PHE A559 7.435 −4.456 27.272 1.00 34.80 ATOM 171 C PHE A 559 3.841 −0.63931.196 1.00 26.88 ATOM 172 O PHE A 559 2.664 −0.631 30.837 1.00 25.97ATOM 173 N SER A 560 4.245 −0.213 32.389 1.00 25.49 ATOM 174 CA SER A560 3.321 0.285 33.407 1.00 26.93 ATOM 175 CB SER A 560 3.945 0.12034.797 1.00 39.67 ATOM 176 OG SER A 560 5.170 0.830 34.899 1.00 40.02ATOM 177 C SER A 560 2.920 1.745 33.197 1.00 26.06 ATOM 178 O SER A 5602.205 2.327 34.018 1.00 26.04 ATOM 179 N PHE A 561 3.382 2.326 32.0981.00 26.05 ATOM 180 CA PHE A 561 3.081 3.711 31.751 1.00 25.67 ATOM 181CB PHE A 561 3.551 3.982 30.321 1.00 26.66 ATOM 182 CG PHE A 561 3.1585.330 29.795 1.00 25.48 ATOM 183 CD1 PHE A 561 3.990 6.430 29.972 1.0026.67 ATOM 184 CD2 PHE A 561 1.948 5.502 29.127 1.00 26.67 ATOM 185 CE1PHE A 561 3.624 7.686 29.489 1.00 26.12 ATOM 186 CE2 PHE A 561 1.5716.748 28.642 1.00 25.76 ATOM 187 CZ PHE A 561 2.412 7.844 28.823 1.0026.46 ATOM 188 C PHE A 561 1.597 4.082 31.865 1.00 26.23 ATOM 189 O PHEA 561 0.715 3.293 31.533 1.00 25.55 ATOM 190 N SER A 562 1.335 5.30432.320 1.00 24.91 ATOM 191 CA SER A 562 −0.029 5.803 32.463 1.00 26.24ATOM 192 CB SER A 562 −0.406 5.906 33.940 1.00 42.72 ATOM 193 OG SER A562 −1.720 6.414 34.084 1.00 43.29 ATOM 194 C SER A 562 −0.134 7.17931.817 1.00 24.23 ATOM 195 O SER A 562 0.730 8.024 32.013 1.00 25.59ATOM 196 N ASP A 563 −1.199 7.401 31.055 1.00 23.00 ATOM 197 CA ASP A563 −1.410 8.675 30.373 1.00 22.76 ATOM 198 CB ASP A 563 −2.135 8.44629.043 1.00 25.24 ATOM 199 CG ASP A 563 −3.635 8.228 29.230 1.00 23.77ATOM 200 OD1 ASP A 563 −4.037 7.150 29.718 1.00 23.35 ATOM 201 OD2 ASP A563 −4.421 9.143 28.906 1.00 24.81 ATOM 202 C ASP A 563 −2.263 9.65931.176 1.00 22.96 ATOM 203 O ASP A 563 −2.297 10.848 30.865 1.00 21.79ATOM 204 N PHE A 564 −2.958 9.150 32.187 1.00 24.29 ATOM 205 CA PHE A564 −3.878 9.962 32.987 1.00 25.23 ATOM 206 CB PHE A 564 −4.394 9.15734.180 1.00 41.24 ATOM 207 CG PHE A 564 −5.576 9.787 34.857 1.00 41.58ATOM 208 CD1 PHE A 564 −6.793 9.895 34.191 1.00 41.99 ATOM 209 CD2 PHE A564 −5.469 10.300 36.146 1.00 42.28 ATOM 210 CE1 PHE A 564 −7.888 10.50634.797 1.00 41.91 ATOM 211 CE2 PHE A 564 −6.558 10.915 36.763 1.00 41.92ATOM 212 CZ PHE A 564 −7.769 11.018 36.086 1.00 41.83 ATOM 213 C PHE A564 −3.410 11.321 33.490 1.00 25.10 ATOM 214 O PHE A 564 −4.185 12.27833.488 1.00 25.27 ATOM 215 N GLU A 565 −2.158 11.406 33.921 1.00 29.45ATOM 216 CA GLU A 565 −1.618 12.651 34.459 1.00 30.36 ATOM 217 CB GLU A565 −0.456 12.341 35.408 1.00 40.02 ATOM 218 CG GLU A 565 −0.821 11.52436.645 1.00 40.24 ATOM 219 CD GLU A 565 −1.312 10.120 36.320 1.00 40.61ATOM 220 OE1 GLU A 565 −0.655 9.424 35.514 1.00 40.05 ATOM 221 OE2 GLU A565 −2.352 9.711 36.883 1.00 40.18 ATOM 222 C GLU A 565 −1.144 13.65233.409 1.00 30.08 ATOM 223 O GLU A 565 −0.860 14.810 33.732 1.00 30.87ATOM 224 N LEU A 566 −1.070 13.217 32.155 1.00 25.91 ATOM 225 CA LEU A566 −0.587 14.073 31.078 1.00 25.51 ATOM 226 CB LEU A 566 0.157 13.21930.051 1.00 30.68 ATOM 227 CG LEU A 566 1.256 12.294 30.578 1.00 31.45ATOM 228 CD1 LEU A 566 1.775 11.429 29.437 1.00 30.44 ATOM 229 CD2 LEU A566 2.377 13.112 31.186 1.00 31.07 ATOM 230 C LEU A 566 −1.642 14.88930.349 1.00 25.31 ATOM 231 O LEU A 566 −2.793 14.475 30.220 1.00 24.57ATOM 232 N SER A 567 −1.228 16.054 29.859 1.00 27.06 ATOM 233 CA SER A567 −2.110 16.928 29.096 1.00 26.87 ATOM 234 CB SER A 567 −1.619 18.37329.159 1.00 26.86 ATOM 235 OG SER A 567 −0.406 18.519 28.439 1.00 26.48ATOM 236 C SER A 567 −2.038 16.447 27.650 1.00 26.54 ATOM 237 O SER A567 −1.187 15.617 27.314 1.00 25.78 ATOM 238 N ASP A 568 −2.921 16.96326.800 1.00 25.65 ATOM 239 CA ASP A 568 −2.935 16.588 25.388 1.00 25.44ATOM 240 CB ASP A 568 −4.077 17.292 24.657 1.00 35.03 ATOM 241 CG ASP A568 −5.437 16.732 25.028 1.00 35.82 ATOM 242 OD1 ASP A 568 −6.450 17.28424.555 1.00 36.02 ATOM 243 OD2 ASP A 568 −5.489 15.744 25.788 1.00 35.24ATOM 244 C ASP A 568 −1.604 16.946 24.739 1.00 26.02 ATOM 245 O ASP A568 −1.040 16.154 23.981 1.00 24.45 ATOM 246 N LEU A 569 −1.104 18.14025.040 1.00 26.56 ATOM 247 CA LEU A 569 0.177 18.584 24.501 1.00 27.05ATOM 248 CB LEU A 569 0.544 19.958 25.066 1.00 35.85 ATOM 249 CG LEU A569 1.958 20.460 24.751 1.00 36.55 ATOM 250 CD1 LEU A 569 2.110 20.68323.255 1.00 36.24 ATOM 251 CD2 LEU A 569 2.211 21.755 25.509 1.00 36.44ATOM 252 C LEU A 569 1.267 17.582 24.864 1.00 25.81 ATOM 253 O LEU A 5692.080 17.214 24.021 1.00 27.30 ATOM 254 N GLU A 570 1.283 17.151 26.1261.00 24.45 ATOM 255 CA GLU A 570 2.266 16.183 26.596 1.00 23.61 ATOM 256CB GLU A 570 2.143 15.984 28.104 1.00 28.33 ATOM 257 CG GLU A 570 2.60017.182 28.912 1.00 28.49 ATOM 258 CD GLU A 570 2.473 16.953 30.402 1.0028.93 ATOM 259 OE1 GLU A 570 1.346 16.679 30.864 1.00 27.96 ATOM 260 OE2GLU A 570 3.500 17.049 31.111 1.00 29.89 ATOM 261 C GLU A 570 2.14914.832 25.892 1.00 23.15 ATOM 262 O GLU A 570 3.166 14.194 25.622 1.0023.63 ATOM 263 N THR A 571 0.931 14.382 25.592 1.00 21.78 ATOM 264 CATHR A 571 0.803 13.099 24.897 1.00 21.61 ATOM 265 CB THR A 571 −0.67012.597 24.814 1.00 20.96 ATOM 266 OG1 THR A 571 −1.477 13.550 24.1171.00 22.41 ATOM 267 CG2 THR A 571 −1.242 12.365 26.212 1.00 20.91 ATOM268 C THR A 571 1.362 13.236 23.483 1.00 22.39 ATOM 269 O THR A 5711.924 12.283 22.929 1.00 21.33 ATOM 270 N ALA A 572 1.218 14.425 22.9061.00 21.89 ATOM 271 CA ALA A 572 1.726 14.683 21.564 1.00 22.51 ATOM 272CB ALA A 572 1.235 16.037 21.061 1.00 23.95 ATOM 273 C ALA A 572 3.24714.647 21.603 1.00 23.15 ATOM 274 O ALA A 572 3.885 14.120 20.690 1.0023.62 ATOM 275 N LEU A 573 3.830 15.211 22.660 1.00 24.60 ATOM 276 CALEU A 573 5.281 15.215 22.805 1.00 25.21 ATOM 277 CB LEU A 573 5.69416.061 24.013 1.00 27.78 ATOM 278 CG LEU A 573 5.470 17.565 23.808 1.0027.76 ATOM 279 CD1 LEU A 573 5.732 18.313 25.101 1.00 27.67 ATOM 280 CD2LEU A 573 6.391 18.074 22.699 1.00 27.52 ATOM 281 C LEU A 573 5.77713.784 22.953 1.00 25.21 ATOM 282 O LEU A 573 6.797 13.413 22.374 1.0025.36 ATOM 283 N CYS A 574 5.052 12.979 23.725 1.00 21.84 ATOM 284 CACYS A 574 5.432 11.581 23.897 1.00 21.46 ATOM 285 CB CYS A 574 4.44610.852 24.807 1.00 23.13 ATOM 286 SG CYS A 574 4.663 11.173 26.560 1.0022.80 ATOM 287 C CYS A 574 5.426 10.890 22.540 1.00 21.90 ATOM 288 O CYSA 574 6.277 10.047 22.260 1.00 21.49 ATOM 289 N THR A 575 4.449 11.24021.705 1.00 23.44 ATOM 290 CA THR A 575 4.334 10.631 20.384 1.00 21.88ATOM 291 CB THR A 575 3.006 11.042 19.699 1.00 21.68 ATOM 292 OG1 THR A575 1.916 10.641 20.536 1.00 22.63 ATOM 293 CG2 THR A 575 2.857 10.37018.340 1.00 22.72 ATOM 294 C THR A 575 5.534 11.000 19.518 1.00 22.93ATOM 295 O THR A 575 6.111 10.140 18.865 1.00 20.91 ATOM 296 N ILE A 5765.929 12.268 19.529 1.00 22.16 ATOM 297 CA ILE A 576 7.091 12.673 18.7481.00 23.75 ATOM 298 CB ILE A 576 7.403 14.171 18.924 1.00 26.26 ATOM 299CG2 ILE A 576 8.756 14.495 18.311 1.00 26.23 ATOM 300 CG1 ILE A 5766.318 15.016 18.260 1.00 26.29 ATOM 301 CD1 ILE A 576 6.476 16.49418.490 1.00 26.83 ATOM 302 C ILE A 576 8.311 11.872 19.209 1.00 22.92ATOM 303 O ILE A 576 9.111 11.416 18.394 1.00 23.77 ATOM 304 N ARG A 5778.447 11.703 20.521 1.00 24.95 ATOM 305 CA ARG A 577 9.575 10.965 21.0771.00 24.47 ATOM 306 CB ARG A 577 9.560 11.050 22.609 1.00 26.95 ATOM 307CG ARG A 577 10.652 10.234 23.294 1.00 27.15 ATOM 308 CD ARG A 57712.031 10.561 22.731 1.00 27.06 ATOM 309 NE ARG A 577 12.398 11.95622.957 1.00 26.65 ATOM 310 CZ ARG A 577 13.447 12.556 22.401 1.00 27.38ATOM 311 NH1 ARG A 577 14.247 11.888 21.578 1.00 27.39 ATOM 312 NH2 ARGA 577 13.696 13.829 22.666 1.00 26.81 ATOM 313 C ARG A 577 9.565 9.50920.625 1.00 24.18 ATOM 314 O ARG A 577 10.619 8.913 20.416 1.00 24.97ATOM 315 N MET A 578 8.372 8.938 20.471 1.00 21.76 ATOM 316 CA MET A 5788.247 7.552 20.032 1.00 21.44 ATOM 317 CB MET A 578 6.782 7.122 20.0421.00 25.13 ATOM 318 CG MET A 578 6.222 6.855 21.425 1.00 23.93 ATOM 319SD MET A 578 4.483 6.363 21.351 1.00 23.95 ATOM 320 CE MET A 578 3.8926.945 22.915 1.00 24.88 ATOM 321 C MET A 578 8.820 7.370 18.630 1.0022.27 ATOM 322 O MET A 578 9.562 6.422 18.373 1.00 22.21 ATOM 323 N PHEA 579 8.462 8.270 17.722 1.00 22.29 ATOM 324 CA PHE A 579 8.960 8.19416.355 1.00 22.58 ATOM 325 CB PHE A 579 8.317 9.267 15.474 1.00 22.36ATOM 326 CG PHE A 579 6.970 8.885 14.925 1.00 22.77 ATOM 327 CD1 PHE A579 5.812 9.077 15.672 1.00 22.73 ATOM 328 CD2 PHE A 579 6.864 8.34113.649 1.00 21.91 ATOM 329 CE1 PHE A 579 4.560 8.733 15.151 1.00 22.92ATOM 330 CE2 PHE A 579 5.625 7.993 13.119 1.00 22.30 ATOM 331 CZ PHE A579 4.469 8.190 13.871 1.00 22.31 ATOM 332 C PHE A 579 10.466 8.39016.328 1.00 24.14 ATOM 333 O PHE A 579 11.183 7.701 15.600 1.00 22.99ATOM 334 N THR A 580 10.935 9.336 17.133 1.00 24.07 ATOM 335 CA THR A580 12.350 9.667 17.198 1.00 24.45 ATOM 336 CB THR A 580 12.567 10.90118.085 1.00 24.15 ATOM 337 OG1 THR A 580 11.712 11.961 17.636 1.00 24.88ATOM 338 CG2 THR A 580 14.008 11.370 18.009 1.00 24.18 ATOM 339 C THR A580 13.239 8.535 17.691 1.00 24.89 ATOM 340 O THR A 580 14.218 8.18817.030 1.00 24.15 ATOM 341 N ASP A 581 12.903 7.955 18.840 1.00 26.03ATOM 342 CA ASP A 581 13.703 6.870 19.402 1.00 26.27 ATOM 343 CB ASP A581 13.395 6.710 20.894 1.00 26.96 ATOM 344 CG ASP A 581 14.029 7.80821.733 1.00 26.96 ATOM 345 OD1 ASP A 581 14.376 8.868 21.167 1.00 26.78ATOM 346 OD2 ASP A 581 14.176 7.620 22.958 1.00 27.14 ATOM 347 C ASP A581 13.578 5.534 18.676 1.00 26.95 ATOM 348 O ASP A 581 14.306 4.58918.978 1.00 27.55 ATOM 349 N LEU A 582 12.654 5.447 17.727 1.00 25.40ATOM 350 CA LEU A 582 12.516 4.231 16.934 1.00 25.74 ATOM 351 CB LEU A582 11.040 3.918 16.642 1.00 23.64 ATOM 352 CG LEU A 582 10.286 3.27417.817 1.00 22.73 ATOM 353 CD1 LEU A 582 8.801 3.146 17.484 1.00 21.47ATOM 354 CD2 LEU A 582 10.873 1.900 18.125 1.00 22.27 ATOM 355 C LEU A582 13.284 4.483 15.635 1.00 26.83 ATOM 356 O LEU A 582 13.259 3.66914.710 1.00 26.36 ATOM 357 N ASN A 583 13.967 5.625 15.588 1.00 30.93ATOM 358 CA ASN A 583 14.767 6.026 14.433 1.00 32.87 ATOM 359 CB ASN A583 15.944 5.065 14.247 1.00 52.34 ATOM 360 CG ASN A 583 17.069 5.33115.225 1.00 53.08 ATOM 361 OD1 ASN A 583 18.026 4.561 15.312 1.00 53.41ATOM 362 ND2 ASN A 583 16.967 6.432 15.962 1.00 53.31 ATOM 363 C ASN A583 13.973 6.114 13.143 1.00 31.76 ATOM 364 O ASN A 583 14.443 5.70612.085 1.00 32.63 ATOM 365 N LEU A 584 12.769 6.665 13.235 1.00 27.18ATOM 366 CA LEU A 584 11.904 6.813 12.073 1.00 27.03 ATOM 367 CB LEU A584 10.455 6.521 12.468 1.00 25.42 ATOM 368 CG LEU A 584 9.877 5.10712.377 1.00 27.73 ATOM 369 CD1 LEU A 584 10.936 4.047 12.537 1.00 26.75ATOM 370 CD2 LEU A 584 8.771 4.975 13.422 1.00 25.52 ATOM 371 C LEU A584 11.971 8.208 11.468 1.00 26.54 ATOM 372 O LEU A 584 11.760 8.38010.270 1.00 27.46 ATOM 373 N VAL A 585 12.265 9.204 12.296 1.00 28.54ATOM 374 CA VAL A 585 12.300 10.589 11.831 1.00 29.02 ATOM 375 CB VAL A585 12.403 11.550 13.025 1.00 27.38 ATOM 376 CG1 VAL A 585 12.404 12.99312.545 1.00 27.75 ATOM 377 CG2 VAL A 585 11.236 11.310 13.971 1.00 27.59ATOM 378 C VAL A 585 13.375 10.951 10.804 1.00 30.26 ATOM 379 O VAL A585 13.059 11.379 9.693 1.00 29.85 ATOM 380 N GLN A 586 14.639 10.79911.167 1.00 36.79 ATOM 381 CA GLN A 586 15.697 11.132 10.228 1.00 38.86ATOM 382 CB GLN A 586 17.024 11.300 10.969 1.00 56.08 ATOM 383 CG GLN A586 16.935 12.315 12.102 1.00 56.46 ATOM 384 CD GLN A 586 18.288 12.83312.551 1.00 56.85 ATOM 385 OE1 GLN A 586 18.393 13.538 13.556 1.00 56.83ATOM 386 NE2 GLN A 586 19.332 12.494 11.801 1.00 56.71 ATOM 387 C GLN A586 15.796 10.046 9.163 1.00 38.13 ATOM 388 O GLN A 586 16.005 10.3367.985 1.00 38.63 ATOM 389 N ASN A 587 15.615 8.799 9.586 1.00 34.73 ATOM390 CA ASN A 587 15.665 7.652 8.685 1.00 34.34 ATOM 391 CB ASN A 58715.120 6.420 9.399 1.00 37.16 ATOM 392 CG ASN A 587 15.340 5.140 8.6201.00 36.75 ATOM 393 OD1 ASN A 587 15.392 5.141 7.389 1.00 36.63 ATOM 394ND2 ASN A 587 15.450 4.031 9.341 1.00 37.09 ATOM 395 C ASN A 587 14.8347.911 7.430 1.00 34.66 ATOM 396 O ASN A 587 15.294 7.691 6.307 1.0034.46 ATOM 397 N PHE A 588 13.600 8.372 7.628 1.00 30.54 ATOM 398 CA PHEA 588 12.711 8.654 6.511 1.00 30.38 ATOM 399 CB PHE A 588 11.366 7.9646.734 1.00 24.15 ATOM 400 CG PHE A 588 11.487 6.479 6.910 1.00 23.77ATOM 401 CD1 PHE A 588 11.369 5.896 8.169 1.00 24.08 ATOM 402 CD2 PHE A588 11.762 5.663 5.820 1.00 23.24 ATOM 403 CE1 PHE A 588 11.526 4.5158.336 1.00 24.41 ATOM 404 CE2 PHE A 588 11.921 4.285 5.969 1.00 23.43ATOM 405 CZ PHE A 588 11.804 3.707 7.228 1.00 23.76 ATOM 406 C PHE A 58812.535 10.151 6.304 1.00 30.36 ATOM 407 O PHE A 588 11.595 10.599 5.6491.00 30.79 ATOM 408 N GLN A 589 13.462 10.912 6.873 1.00 35.42 ATOM 409CA GLN A 589 13.489 12.366 6.750 1.00 36.58 ATOM 410 CB GLN A 589 14.16712.739 5.433 1.00 49.72 ATOM 411 CG GLN A 589 15.501 12.043 5.243 1.0049.96 ATOM 412 CD GLN A 589 15.680 11.505 3.839 1.00 50.27 ATOM 413 OE1GLN A 589 14.788 10.852 3.296 1.00 50.16 ATOM 414 NE2 GLN A 589 16.83911.762 3.249 1.00 50.04 ATOM 415 C GLN A 589 12.133 13.055 6.846 1.0036.29 ATOM 416 O GLN A 589 11.648 13.655 5.882 1.00 36.29 ATOM 417 N META 590 11.524 12.969 8.021 1.00 36.14 ATOM 418 CA MET A 590 10.240 13.6088.258 1.00 35.67 ATOM 419 CB MET A 590 9.459 12.847 9.331 1.00 32.44ATOM 420 CG MET A 590 9.055 11.431 8.966 1.00 31.88 ATOM 421 SD MET A590 8.254 10.607 10.373 1.00 31.19 ATOM 422 CE MET A 590 6.882 11.64110.615 1.00 32.88 ATOM 423 C MET A 590 10.515 15.022 8.759 1.00 35.35ATOM 424 O MET A 590 11.351 15.209 9.641 1.00 35.80 ATOM 425 N LYS A 5919.839 16.014 8.191 1.00 35.07 ATOM 426 CA LYS A 591 10.016 17.389 8.6481.00 34.67 ATOM 427 CB LYS A 591 9.427 18.381 7.641 1.00 46.77 ATOM 428CG LYS A 591 10.350 18.721 6.480 1.00 47.35 ATOM 429 CD LYS A 591 10.65017.509 5.612 1.00 47.48 ATOM 430 CE LYS A 591 11.738 17.813 4.587 1.0047.57 ATOM 431 NZ LYS A 591 11.398 18.958 3.694 1.00 47.52 ATOM 432 CLYS A 591 9.274 17.492 9.976 1.00 33.93 ATOM 433 O LYS A 591 8.13217.049 10.081 1.00 34.06 ATOM 434 N HIS A 592 9.926 18.068 10.983 1.0027.75 ATOM 435 CA HIS A 592 9.332 18.205 12.310 1.00 26.86 ATOM 436 CBHIS A 592 10.227 19.071 13.208 1.00 27.82 ATOM 437 CG HIS A 592 9.77019.139 14.632 1.00 26.72 ATOM 438 CD2 HIS A 592 9.317 20.178 15.374 1.0027.57 ATOM 439 ND1 HIS A 592 9.755 18.040 15.464 1.00 27.40 ATOM 440 CE1HIS A 592 9.314 18.399 16.657 1.00 27.96 ATOM 441 NE2 HIS A 592 9.04119.692 16.628 1.00 27.67 ATOM 442 C HIS A 592 7.927 18.796 12.277 1.0028.09 ATOM 443 O HIS A 592 7.021 18.288 12.933 1.00 26.68 ATOM 444 N GLUA 593 7.749 19.865 11.508 1.00 32.89 ATOM 445 CA GLU A 593 6.456 20.53411.405 1.00 34.01 ATOM 446 CB GLU A 593 6.572 21.771 10.510 1.00 53.17ATOM 447 CG GLU A 593 7.483 22.870 11.051 1.00 53.98 ATOM 448 CD GLU A593 8.914 22.403 11.272 1.00 54.08 ATOM 449 OE1 GLU A 593 9.519 21.85310.326 1.00 53.79 ATOM 450 OE2 GLU A 593 9.434 22.591 12.394 1.00 53.97ATOM 451 C GLU A 593 5.370 19.613 10.856 1.00 33.01 ATOM 452 O GLU A 5934.230 19.634 11.319 1.00 32.84 ATOM 453 N VAL A 594 5.730 18.808 9.8641.00 27.04 ATOM 454 CA VAL A 594 4.783 17.886 9.249 1.00 25.85 ATOM 455CB VAL A 594 5.382 17.279 7.962 1.00 24.72 ATOM 456 CG1 VAL A 594 4.44616.233 7.381 1.00 24.57 ATOM 457 CG2 VAL A 594 5.631 18.383 6.945 1.0024.02 ATOM 458 C VAL A 594 4.386 16.771 10.215 1.00 26.36 ATOM 459 O VALA 594 3.214 16.386 10.283 1.00 25.05 ATOM 460 N LEU A 595 5.356 16.24610.956 1.00 24.15 ATOM 461 CA LEU A 595 5.062 15.187 11.918 1.00 25.41ATOM 462 CB LEU A 595 6.352 14.633 12.536 1.00 24.61 ATOM 463 CG LEU A595 6.204 13.640 13.696 1.00 25.86 ATOM 464 CD1 LEU A 595 5.345 12.45313.272 1.00 24.75 ATOM 465 CD2 LEU A 595 7.577 13.163 14.141 1.00 25.05ATOM 466 C LEU A 595 4.148 15.745 13.009 1.00 25.02 ATOM 467 O LEU A 5953.197 15.088 13.435 1.00 24.20 ATOM 468 N CYS A 596 4.426 16.970 13.4511.00 24.36 ATOM 469 CA CYS A 596 3.603 17.588 14.479 1.00 24.03 ATOM 470CB CYS A 596 4.195 18.931 14.907 1.00 27.15 ATOM 471 SG CYS A 596 5.69918.771 15.892 1.00 26.30 ATOM 472 C CYS A 596 2.177 17.789 13.987 1.0024.31 ATOM 473 O CYS A 596 1.222 17.537 14.721 1.00 24.29 ATOM 474 N ARGA 597 2.032 18.233 12.742 1.00 22.43 ATOM 475 CA ARG A 597 0.703 18.46012.194 1.00 22.27 ATOM 476 CB ARG A 597 0.777 19.177 10.841 1.00 37.36ATOM 477 CG ARG A 597 −0.597 19.576 10.315 1.00 38.44 ATOM 478 CD ARG A597 −0.541 20.392 9.032 1.00 38.82 ATOM 479 NE ARG A 597 0.033 21.7199.233 1.00 38.78 ATOM 480 CZ ARG A 597 1.286 22.043 8.936 1.00 38.71ATOM 481 NH1 ARG A 597 2.101 21.133 8.421 1.00 38.58 ATOM 482 NH2 ARG A597 1.721 23.278 9.149 1.00 38.90 ATOM 483 C ARG A 597 −0.042 17.14012.042 1.00 21.87 ATOM 484 O ARG A 597 −1.231 17.049 12.347 1.00 22.25ATOM 485 N TRP A 598 0.661 16.114 11.578 1.00 22.62 ATOM 486 CA TRP A598 0.039 14.802 11.396 1.00 20.68 ATOM 487 CB TRP A 598 1.048 13.82610.788 1.00 21.19 ATOM 488 CG TRP A 598 0.506 12.443 10.641 1.00 20.61ATOM 489 CD2 TRP A 598 0.680 11.358 11.554 1.00 21.45 ATOM 490 CE2 TRP A598 −0.059 10.262 11.048 1.00 20.54 ATOM 491 CE3 TRP A 598 1.386 11.20112.755 1.00 20.69 ATOM 492 CD1 TRP A 598 −0.304 11.982 9.644 1.00 21.12ATOM 493 NE1 TRP A 598 −0.648 10.671 9.882 1.00 21.75 ATOM 494 CZ2 TRP A598 −0.111 9.028 11.701 1.00 20.03 ATOM 495 CZ3 TRP A 598 1.334 9.97413.406 1.00 21.23 ATOM 496 CH2 TRP A 598 0.588 8.901 12.875 1.00 21.56ATOM 497 C TRP A 598 −0.461 14.256 12.734 1.00 20.83 ATOM 498 O TRP A598 −1.575 13.743 12.833 1.00 20.85 ATOM 499 N ILE A 599 0.371 14.36213.762 1.00 18.38 ATOM 500 CA ILE A 599 −0.001 13.881 15.081 1.00 17.01ATOM 501 CB ILE A 599 1.138 14.106 16.103 1.00 18.07 ATOM 502 CG2 ILE A599 0.625 13.881 17.516 1.00 18.87 ATOM 503 CG1 ILE A 599 2.304 13.15815.794 1.00 18.94 ATOM 504 CD1 ILE A 599 3.523 13.367 16.669 1.00 18.33ATOM 505 C ILE A 599 −1.263 14.596 15.554 1.00 18.40 ATOM 506 O ILE A599 −2.184 13.969 16.081 1.00 16.74 ATOM 507 N LEU A 600 −1.311 15.91215.371 1.00 21.06 ATOM 508 CA LEU A 600 −2.486 16.657 15.802 1.00 21.13ATOM 509 CB LEU A 600 −2.202 18.162 15.761 1.00 21.76 ATOM 510 CG LEU A600 −1.149 18.582 16.788 1.00 21.76 ATOM 511 CD1 LEU A 600 −0.811 20.05316.597 1.00 21.85 ATOM 512 CD2 LEU A 600 −1.672 18.324 18.201 1.00 22.51ATOM 513 C LEU A 600 −3.728 16.325 14.979 1.00 20.73 ATOM 514 O LEU A600 −4.841 16.351 15.501 1.00 21.49 ATOM 515 N SER A 601 −3.540 16.03213.694 1.00 21.08 ATOM 516 CA SER A 601 −4.665 15.674 12.833 1.00 20.75ATOM 517 CB SER A 601 −4.225 15.579 11.372 1.00 22.55 ATOM 518 OG SER A601 −4.008 16.869 10.822 1.00 23.14 ATOM 519 C SER A 601 −5.228 14.33313.287 1.00 20.19 ATOM 520 O SER A 601 −6.438 14.125 13.275 1.00 20.13ATOM 521 N VAL A 602 −4.340 13.424 13.679 1.00 21.43 ATOM 522 CA VAL A602 −4.773 12.116 14.168 1.00 21.85 ATOM 523 CB VAL A 602 −3.564 11.20414.471 1.00 17.69 ATOM 524 CG1 VAL A 602 −4.018 9.928 15.198 1.00 18.88ATOM 525 CG2 VAL A 602 −2.867 10.845 13.174 1.00 19.25 ATOM 526 C VAL A602 −5.581 12.312 15.445 1.00 21.58 ATOM 527 O VAL A 602 −6.705 11.82315.566 1.00 20.63 ATOM 528 N LYS A 603 −5.011 13.052 16.394 1.00 20.30ATOM 529 CA LYS A 603 −5.697 13.303 17.655 1.00 19.93 ATOM 530 CB LYS A603 −4.833 14.186 18.567 1.00 29.59 ATOM 531 CG LYS A 603 −5.553 14.66319.829 1.00 29.47 ATOM 532 CD LYS A 603 −4.587 15.206 20.882 1.00 30.01ATOM 533 CE LYS A 603 −3.846 16.449 20.416 1.00 30.55 ATOM 534 NZ LYS A603 −2.899 16.934 21.464 1.00 31.23 ATOM 535 C LYS A 603 −7.052 13.96817.430 1.00 19.43 ATOM 536 O LYS A 603 −8.034 13.636 18.095 1.00 20.76ATOM 537 N LYS A 604 −7.100 14.894 16.481 1.00 19.98 ATOM 538 CA LYS A604 −8.325 15.629 16.174 1.00 21.57 ATOM 539 CB LYS A 604 −8.024 16.77515.207 1.00 38.76 ATOM 540 CG LYS A 604 −9.262 17.531 14.741 1.00 39.38ATOM 541 CD LYS A 604 −8.910 18.610 13.732 1.00 39.39 ATOM 542 CE LYS A604 −10.158 19.340 13.255 1.00 39.74 ATOM 543 NZ LYS A 604 −9.843 20.38512.242 1.00 39.72 ATOM 544 C LYS A 604 −9.413 14.754 15.579 1.00 20.90ATOM 545 O LYS A 604 −10.609 15.039 15.742 1.00 21.11 ATOM 546 N ASN A605 −9.009 13.688 14.892 1.00 21.37 ATOM 547 CA ASN A 605 −9.987 12.81214.273 1.00 21.04 ATOM 548 CB ASN A 605 −9.486 12.315 12.920 1.00 27.07ATOM 549 CG ASN A 605 −9.635 13.366 11.836 1.00 27.98 ATOM 550 OD1 ASN A605 −8.775 14.234 11.666 1.00 27.85 ATOM 551 ND2 ASN A 605 −10.74513.308 11.112 1.00 27.52 ATOM 552 C ASN A 605 −10.506 11.662 15.116 1.0021.57 ATOM 553 O ASN A 605 −11.072 10.702 14.590 1.00 23.07 ATOM 554 NTYR A 606 −10.292 11.754 16.422 1.00 20.07 ATOM 555 CA TYR A 606 −10.85310.792 17.349 1.00 20.46 ATOM 556 CB TYR A 606 −9.858 10.374 18.437 1.0018.79 ATOM 557 CG TYR A 606 −8.993 9.216 17.992 1.00 18.19 ATOM 558 CD1TYR A 606 −7.745 9.430 17.409 1.00 19.08 ATOM 559 CE1 TYR A 606 −6.9898.362 16.913 1.00 18.94 ATOM 560 CD2 TYR A 606 −9.467 7.909 18.074 1.0018.23 ATOM 561 CE2 TYR A 606 −8.722 6.840 17.578 1.00 17.63 ATOM 562 CZTYR A 606 −7.485 7.077 16.999 1.00 18.23 ATOM 563 OH TYR A 606 −6.7476.029 16.489 1.00 15.86 ATOM 564 C TYR A 606 −12.015 11.580 17.947 1.0021.76 ATOM 565 O TYR A 606 −11.975 12.819 18.007 1.00 20.70 ATOM 566 NARG A 607 −13.060 10.882 18.365 1.00 19.57 ATOM 567 CA ARG A 607 −14.22311.562 18.931 1.00 20.12 ATOM 568 CB ARG A 607 −15.497 10.791 18.5751.00 23.54 ATOM 569 CG ARG A 607 −15.679 10.605 17.074 1.00 23.38 ATOM570 CD ARG A 607 −17.034 10.010 16.715 1.00 23.37 ATOM 571 NE ARG A 607−17.142 9.734 15.282 1.00 24.11 ATOM 572 CZ ARG A 607 −18.274 9.40814.665 1.00 24.11 ATOM 573 NH1 ARG A 607 −19.405 9.321 15.355 1.00 24.42ATOM 574 NH2 ARG A 607 −18.274 9.163 13.362 1.00 25.10 ATOM 575 C ARG A607 −14.037 11.647 20.438 1.00 20.33 ATOM 576 O ARG A 607 −14.168 10.64821.150 1.00 20.09 ATOM 577 N LYS A 608 −13.736 12.847 20.926 1.00 25.24ATOM 578 CA LYS A 608 −13.484 13.033 22.349 1.00 25.95 ATOM 579 CB LYS A608 −13.108 14.491 22.636 1.00 41.13 ATOM 580 CG LYS A 608 −14.17515.511 22.294 1.00 41.73 ATOM 581 CD LYS A 608 −13.670 16.916 22.6031.00 41.87 ATOM 582 CE LYS A 608 −14.750 17.972 22.413 1.00 41.79 ATOM583 NZ LYS A 608 −14.231 19.340 22.703 1.00 41.73 ATOM 584 C LYS A 608−14.625 12.599 23.254 1.00 26.44 ATOM 585 O LYS A 608 −14.397 12.22524.405 1.00 25.96 ATOM 586 N ASN A 609 −15.847 12.626 22.732 1.00 27.23ATOM 587 CA ASN A 609 −17.005 12.248 23.522 1.00 27.32 ATOM 588 CB ASN A609 −18.212 13.066 23.071 1.00 36.30 ATOM 589 CG ASN A 609 −17.99514.554 23.282 1.00 36.84 ATOM 590 OD1 ASN A 609 −17.809 15.008 24.4111.00 37.02 ATOM 591 ND2 ASN A 609 −17.998 15.316 22.199 1.00 37.30 ATOM592 C ASN A 609 −17.317 10.758 23.541 1.00 26.80 ATOM 593 O ASN A 609−18.330 10.332 24.098 1.00 27.72 ATOM 594 N VAL A 610 −16.451 9.96422.920 1.00 21.65 ATOM 595 CA VAL A 610 −16.616 8.512 22.946 1.00 20.92ATOM 596 CB VAL A 610 −16.097 7.862 21.645 1.00 20.35 ATOM 597 CG1 VAL A610 −15.897 6.370 21.846 1.00 20.76 ATOM 598 CG2 VAL A 610 −17.120 8.08620.522 1.00 18.26 ATOM 599 C VAL A 610 −15.780 8.109 24.171 1.00 19.89ATOM 600 O VAL A 610 −14.590 8.414 24.254 1.00 20.96 ATOM 601 N ALA A611 −16.423 7.450 25.130 1.00 19.80 ATOM 602 CA ALA A 611 −15.791 7.07826.397 1.00 19.90 ATOM 603 CB ALA A 611 −16.780 6.287 27.251 1.00 20.34ATOM 604 C ALA A 611 −14.448 6.363 26.383 1.00 19.34 ATOM 605 O ALA A611 −13.549 6.731 27.138 1.00 20.80 ATOM 606 N TYR A 612 −14.307 5.34325.542 1.00 18.10 ATOM 607 CA TYR A 612 −13.060 4.599 25.512 1.00 15.69ATOM 608 CB TYR A 612 −13.321 3.134 25.873 1.00 20.49 ATOM 609 CG TYR A612 −12.107 2.251 25.709 1.00 20.53 ATOM 610 CD1 TYR A 612 −12.047 1.30424.685 1.00 21.50 ATOM 611 CE1 TYR A 612 −10.932 0.484 24.536 1.00 20.27ATOM 612 CD2 TYR A 612 −11.020 2.359 26.577 1.00 20.70 ATOM 613 CE2 TYRA 612 −9.906 1.546 26.434 1.00 19.44 ATOM 614 CZ TYR A 612 −9.870 0.61125.414 1.00 20.76 ATOM 615 OH TYR A 612 −8.769 −0.205 25.284 1.00 20.43ATOM 616 C TYR A 612 −12.264 4.682 24.218 1.00 14.59 ATOM 617 O TYR A612 −11.064 4.921 24.268 1.00 15.21 ATOM 618 N HIS A 613 −12.915 4.50023.069 1.00 16.35 ATOM 619 CA HIS A 613 −12.197 4.553 21.793 1.00 15.66ATOM 620 CB HIS A 613 −12.942 3.763 20.705 1.00 19.05 ATOM 621 CG HIS A613 −12.971 2.286 20.941 1.00 21.28 ATOM 622 CD2 HIS A 613 −12.010 1.34120.797 1.00 20.01 ATOM 623 ND1 HIS A 613 −14.087 1.628 21.408 1.00 19.61ATOM 624 CE1 HIS A 613 −13.816 0.342 21.541 1.00 20.40 ATOM 625 NE2 HISA 613 −12.562 0.140 21.176 1.00 20.73 ATOM 626 C HIS A 613 −11.998 5.98921.330 1.00 15.17 ATOM 627 O HIS A 613 −12.633 6.451 20.376 1.00 17.00ATOM 628 N ASN A 614 −11.101 6.682 22.020 1.00 18.64 ATOM 629 CA ASN A614 −10.784 8.068 21.725 1.00 17.28 ATOM 630 CB ASN A 614 −11.344 8.97722.827 1.00 21.97 ATOM 631 CG ASN A 614 −10.939 8.530 24.219 1.00 21.21ATOM 632 OD1 ASN A 614 −9.752 8.417 24.526 1.00 22.66 ATOM 633 ND2 ASN A614 −11.928 8.277 25.074 1.00 21.32 ATOM 634 C ASN A 614 −9.265 8.20721.628 1.00 18.30 ATOM 635 O ASN A 614 −8.543 7.210 21.671 1.00 17.11ATOM 636 N TRP A 615 −8.773 9.434 21.504 1.00 20.23 ATOM 637 CA TRP A615 −7.335 9.650 21.388 1.00 20.84 ATOM 638 CB TRP A 615 −7.020 11.15221.346 1.00 18.84 ATOM 639 CG TRP A 615 −5.567 11.469 21.610 1.00 20.81ATOM 640 CD2 TRP A 615 −4.446 11.146 20.775 1.00 20.87 ATOM 641 CE2 TRPA 615 −3.287 11.632 21.427 1.00 20.24 ATOM 642 CE3 TRP A 615 −4.30710.493 19.542 1.00 20.69 ATOM 643 CD1 TRP A 615 −5.055 12.115 22.7001.00 19.88 ATOM 644 NE1 TRP A 615 −3.689 12.217 22.599 1.00 19.37 ATOM645 CZ2 TRP A 615 −2.007 11.488 20.886 1.00 21.34 ATOM 646 CZ3 TRP A 615−3.031 10.346 19.004 1.00 21.28 ATOM 647 CH2 TRP A 615 −1.897 10.84519.679 1.00 21.14 ATOM 648 C TRP A 615 −6.457 8.993 22.453 1.00 19.80ATOM 649 O TRP A 615 −5.383 8.479 22.133 1.00 19.45 ATOM 650 N ARG A 616−6.888 9.010 23.713 1.00 19.15 ATOM 651 CA ARG A 616 −6.063 8.424 24.7641.00 18.73 ATOM 652 CB ARG A 616 −6.658 8.707 26.146 1.00 20.84 ATOM 653CG ARG A 616 −6.628 10.197 26.516 1.00 20.98 ATOM 654 CD ARG A 616−5.208 10.754 26.511 1.00 21.78 ATOM 655 NE ARG A 616 −5.185 12.19526.772 1.00 22.05 ATOM 656 CZ ARG A 616 −4.519 12.760 27.773 1.00 22.62ATOM 657 NH1 ARG A 616 −3.820 12.012 28.610 1.00 22.11 ATOM 658 NH2 ARGA 616 −4.558 14.074 27.936 1.00 22.34 ATOM 659 C ARG A 616 −5.869 6.92224.559 1.00 18.23 ATOM 660 O ARG A 616 −4.799 6.388 24.857 1.00 18.43ATOM 661 N HIS A 617 −6.889 6.246 24.041 1.00 17.23 ATOM 662 CA HIS A617 −6.754 4.812 23.796 1.00 17.41 ATOM 663 CB HIS A 617 −8.095 4.19423.403 1.00 16.86 ATOM 664 CG HIS A 617 −7.964 2.830 22.798 1.00 13.76ATOM 665 CD2 HIS A 617 −8.291 2.369 21.569 1.00 17.85 ATOM 666 ND1 HIS A617 −7.384 1.772 23.465 1.00 17.12 ATOM 667 CE1 HIS A 617 −7.357 0.71622.670 1.00 15.55 ATOM 668 NE2 HIS A 617 −7.899 1.052 21.515 1.00 16.82ATOM 669 C HIS A 617 −5.737 4.566 22.682 1.00 17.79 ATOM 670 O HIS A 617−4.911 3.643 22.770 1.00 17.66 ATOM 671 N ALA A 618 −5.807 5.384 21.6351.00 16.69 ATOM 672 CA ALA A 618 −4.897 5.268 20.499 1.00 17.60 ATOM 673CB ALA A 618 −5.268 6.270 19.416 1.00 19.06 ATOM 674 C ALA A 618 −3.4785.517 20.973 1.00 18.60 ATOM 675 O ALA A 618 −2.553 4.777 20.642 1.0016.65 ATOM 676 N PHE A 619 −3.327 6.573 21.764 1.00 16.36 ATOM 677 CAPHE A 619 −2.040 6.942 22.316 1.00 18.60 ATOM 678 CB PHE A 619 −2.2058.224 23.142 1.00 21.01 ATOM 679 CG PHE A 619 −0.989 8.594 23.938 1.0022.31 ATOM 680 CD1 PHE A 619 0.166 9.041 23.305 1.00 21.99 ATOM 681 CD2PHE A 619 −0.995 8.475 25.326 1.00 22.04 ATOM 682 CE1 PHE A 619 1.3049.366 24.045 1.00 21.42 ATOM 683 CE2 PHE A 619 0.139 8.798 26.076 1.0021.94 ATOM 684 CZ PHE A 619 1.292 9.246 25.426 1.00 21.32 ATOM 685 C PHEA 619 −1.459 5.816 23.176 1.00 17.86 ATOM 686 O PHE A 619 −0.285 5.47023.040 1.00 17.74 ATOM 687 N ASN A 620 −2.281 5.239 24.049 1.00 17.68ATOM 688 CA ASN A 620 −1.814 4.160 24.920 1.00 18.84 ATOM 689 CB ASN A620 −2.868 3.793 25.972 1.00 22.20 ATOM 690 CG ASN A 620 −3.028 4.86727.037 1.00 22.41 ATOM 691 OD1 ASN A 620 −2.078 5.578 27.354 1.00 22.93ATOM 692 ND2 ASN A 620 −4.220 4.969 27.611 1.00 21.57 ATOM 693 C ASN A620 −1.450 2.921 24.113 1.00 18.91 ATOM 694 O ASN A 620 −0.514 2.20124.461 1.00 18.42 ATOM 695 N THR A 621 −2.184 2.682 23.031 1.00 16.41ATOM 696 CA THR A 621 −1.901 1.519 22.191 1.00 16.82 ATOM 697 CB THR A621 −2.965 1.360 21.093 1.00 17.95 ATOM 698 OG1 THR A 621 −4.246 1.19021.704 1.00 17.42 ATOM 699 CG2 THR A 621 −2.664 0.130 20.233 1.00 17.02ATOM 700 C THR A 621 −0.526 1.693 21.556 1.00 18.34 ATOM 701 O THR A 6210.276 0.749 21.505 1.00 18.19 ATOM 702 N ALA A 622 −0.249 2.901 21.0851.00 15.98 ATOM 703 CA ALA A 622 1.041 3.211 20.479 1.00 18.35 ATOM 704CB ALA A 622 1.005 4.592 19.864 1.00 16.90 ATOM 705 C ALA A 622 2.1513.138 21.529 1.00 17.61 ATOM 706 O ALA A 622 3.242 2.656 21.248 1.0016.57 ATOM 707 N GLN A 623 1.876 3.622 22.740 1.00 17.78 ATOM 708 CA GLNA 623 2.878 3.578 23.803 1.00 19.17 ATOM 709 CB GLN A 623 2.351 4.26025.071 1.00 19.99 ATOM 710 CG GLN A 623 3.361 4.335 26.219 1.00 19.42ATOM 711 CD GLN A 623 3.358 3.103 27.110 1.00 20.35 ATOM 712 OE1 GLN A623 2.302 2.595 27.488 1.00 19.39 ATOM 713 NE2 GLN A 623 4.547 2.63427.475 1.00 19.48 ATOM 714 C GLN A 623 3.251 2.137 24.114 1.00 19.45ATOM 715 O GLN A 623 4.420 1.824 24.358 1.00 19.89 ATOM 716 N CYS A 6242.258 1.256 24.118 1.00 17.26 ATOM 717 CA CYS A 624 2.533 −0.146 24.3851.00 19.37 ATOM 718 CB CYS A 624 1.234 −0.938 24.530 1.00 19.88 ATOM 719SG CYS A 624 1.499 −2.658 25.026 1.00 19.62 ATOM 720 C CYS A 624 3.369−0.708 23.237 1.00 18.34 ATOM 721 O CYS A 624 4.255 −1.528 23.460 1.0018.71 ATOM 722 N MET A 625 3.094 −0.258 22.015 1.00 19.30 ATOM 723 CAMET A 625 3.844 −0.720 20.843 1.00 18.88 ATOM 724 CB MET A 625 3.259−0.102 19.567 1.00 21.69 ATOM 725 CG MET A 625 3.952 −0.521 18.267 1.0019.33 ATOM 726 SD MET A 625 3.854 −2.291 17.926 1.00 18.96 ATOM 727 CEMET A 625 2.148 −2.414 17.292 1.00 20.28 ATOM 728 C MET A 625 5.307−0.296 21.019 1.00 20.73 ATOM 729 O MET A 625 6.226 −1.097 20.832 1.0019.61 ATOM 730 N PHE A 626 5.515 0.968 21.381 1.00 21.46 ATOM 731 CA PHEA 626 6.862 1.487 21.604 1.00 22.24 ATOM 732 CB PHE A 626 6.810 2.97322.003 1.00 18.30 ATOM 733 CG PHE A 626 8.162 3.566 22.325 1.00 18.77ATOM 734 CD1 PHE A 626 8.662 3.539 23.628 1.00 19.77 ATOM 735 CD2 PHE A626 8.943 4.126 21.321 1.00 19.03 ATOM 736 CE1 PHE A 626 9.920 4.06023.921 1.00 19.58 ATOM 737 CE2 PHE A 626 10.207 4.650 21.607 1.00 19.50ATOM 738 CZ PHE A 626 10.693 4.616 22.907 1.00 17.99 ATOM 739 C PHE A626 7.578 0.684 22.685 1.00 22.81 ATOM 740 O PHE A 626 8.747 0.32122.528 1.00 22.67 ATOM 741 N ALA A 627 6.878 0.405 23.781 1.00 23.57ATOM 742 CA ALA A 627 7.460 −0.351 24.883 1.00 24.17 ATOM 743 CB ALA A627 6.511 −0.357 26.082 1.00 26.38 ATOM 744 C ALA A 627 7.794 −1.78724.477 1.00 24.26 ATOM 745 O ALA A 627 8.854 −2.305 24.834 1.00 25.36ATOM 746 N ALA A 628 6.898 −2.428 23.728 1.00 21.99 ATOM 747 CA ALA A628 7.127 −3.806 23.296 1.00 22.22 ATOM 748 CB ALA A 628 5.884 −4.36422.609 1.00 18.57 ATOM 749 C ALA A 628 8.315 −3.879 22.350 1.00 23.09ATOM 750 O ALA A 628 9.085 −4.838 22.382 1.00 22.87 ATOM 751 N LEU A 6298.462 −2.864 21.506 1.00 21.79 ATOM 752 CA LEU A 629 9.565 −2.835 20.5551.00 24.56 ATOM 753 CB LEU A 629 9.338 −1.737 19.521 1.00 24.39 ATOM 754CG LEU A 629 8.155 −1.980 18.582 1.00 25.70 ATOM 755 CD1 LEU A 629 7.906−0.753 17.734 1.00 25.30 ATOM 756 CD2 LEU A 629 8.446 −3.200 17.711 1.0026.08 ATOM 757 C LEU A 629 10.897 −2.608 21.256 1.00 25.12 ATOM 758 OLEU A 629 11.898 −3.243 20.920 1.00 25.35 ATOM 759 N LYS A 630 10.907−1.705 22.234 1.00 32.90 ATOM 760 CA LYS A 630 12.126 −1.394 22.981 1.0033.87 ATOM 761 CB LYS A 630 12.033 0.012 23.573 1.00 31.73 ATOM 762 CGLYS A 630 12.137 1.116 22.544 1.00 31.51 ATOM 763 CD LYS A 630 13.4941.089 21.868 1.00 32.17 ATOM 764 CE LYS A 630 13.682 2.292 20.966 1.0031.52 ATOM 765 NZ LYS A 630 14.984 2.243 20.254 1.00 31.88 ATOM 766 CLYS A 630 12.416 −2.394 24.096 1.00 34.55 ATOM 767 O LYS A 630 13.176−3.347 23.906 1.00 35.07 ATOM 768 N ALA A 631 11.814 −2.168 25.260 1.0030.54 ATOM 769 CA ALA A 631 12.005 −3.047 26.406 1.00 30.93 ATOM 770 CBALA A 631 11.175 −2.548 27.590 1.00 31.25 ATOM 771 C ALA A 631 11.630−4.492 26.070 1.00 30.76 ATOM 772 O ALA A 631 12.270 −5.432 26.538 1.0030.38 ATOM 773 N GLY A 632 10.588 −4.660 25.257 1.00 30.21 ATOM 774 CAGLY A 632 10.147 −5.991 24.871 1.00 30.31 ATOM 775 C GLY A 632 11.073−6.644 23.860 1.00 30.73 ATOM 776 O GLY A 632 10.975 −7.843 23.592 1.0030.32 ATOM 777 N LYS A 633 11.967 −5.848 23.287 1.00 31.93 ATOM 778 CALYS A 633 12.937 −6.346 22.315 1.00 32.77 ATOM 779 CB LYS A 633 13.858−7.374 22.979 1.00 44.15 ATOM 780 CG LYS A 633 14.875 −6.775 23.929 1.0044.47 ATOM 781 CD LYS A 633 15.841 −7.835 24.426 1.00 44.54 ATOM 782 CELYS A 633 17.052 −7.197 25.079 1.00 44.74 ATOM 783 NZ LYS A 633 17.770−6.316 24.114 1.00 44.90 ATOM 784 C LYS A 633 12.352 −6.948 21.041 1.0032.00 ATOM 785 O LYS A 633 12.862 −7.944 20.522 1.00 32.88 ATOM 786 NILE A 634 11.292 −6.338 20.527 1.00 26.60 ATOM 787 CA ILE A 634 10.670−6.818 19.305 1.00 25.39 ATOM 788 CB ILE A 634 9.124 −6.695 19.400 1.0026.41 ATOM 789 CG2 ILE A 634 8.473 −7.074 18.076 1.00 27.54 ATOM 790 CG1ILE A 634 8.607 −7.612 20.510 1.00 27.29 ATOM 791 CD1 ILE A 634 7.113−7.543 20.725 1.00 27.31 ATOM 792 C ILE A 634 11.200 −6.013 18.117 1.0025.00 ATOM 793 O ILE A 634 11.127 −6.446 16.968 1.00 25.10 ATOM 794 NGLN A 635 11.770 −4.850 18.409 1.00 23.96 ATOM 795 CA GLN A 635 12.305−3.975 17.377 1.00 23.37 ATOM 796 CB GLN A 635 12.904 −2.716 18.010 1.0027.98 ATOM 797 CG GLN A 635 13.476 −1.740 17.002 1.00 28.57 ATOM 798 CDGLN A 635 14.111 −0.516 17.645 1.00 28.17 ATOM 799 OE1 GLN A 635 14.6350.354 16.953 1.00 29.49 ATOM 800 NE2 GLN A 635 14.059 −0.444 18.967 1.0027.30 ATOM 801 C GLN A 635 13.368 −4.672 16.535 1.00 24.49 ATOM 802 OGLN A 635 13.445 −4.468 15.324 1.00 24.24 ATOM 803 N ASN A 636 14.180−5.493 17.195 1.00 30.08 ATOM 804 CA ASN A 636 15.266 −6.222 16.547 1.0031.17 ATOM 805 CB ASN A 636 16.172 −6.829 17.618 1.00 31.58 ATOM 806 CGASN A 636 16.612 −5.811 18.651 1.00 32.71 ATOM 807 OD1 ASN A 636 17.739−5.309 18.607 1.00 32.53 ATOM 808 ND2 ASN A 636 15.716 −5.490 19.5851.00 31.94 ATOM 809 C ASN A 636 14.782 −7.330 15.617 1.00 31.51 ATOM 810O ASN A 636 15.553 −7.853 14.809 1.00 31.97 ATOM 811 N LYS A 637 13.510−7.690 15.732 1.00 28.95 ATOM 812 CA LYS A 637 12.944 −8.750 14.904 1.0028.44 ATOM 813 CB LYS A 637 11.983 −9.596 15.740 1.00 31.06 ATOM 814 CGLYS A 637 12.590 −10.196 16.993 1.00 30.31 ATOM 815 CD LYS A 637 11.502−10.770 17.889 1.00 30.88 ATOM 816 CE LYS A 637 12.072 −11.316 19.1861.00 31.13 ATOM 817 NZ LYS A 637 12.956 −12.494 18.960 1.00 31.42 ATOM818 C LYS A 637 12.200 −8.219 13.683 1.00 28.47 ATOM 819 O LYS A 63711.696 −9.003 12.875 1.00 29.67 ATOM 820 N LEU A 638 12.137 −6.89813.539 1.00 27.41 ATOM 821 CA LEU A 638 11.401 −6.297 12.427 1.00 27.76ATOM 822 CB LEU A 638 10.187 −5.546 12.977 1.00 24.26 ATOM 823 CG LEU A638 9.349 −6.293 14.016 1.00 24.56 ATOM 824 CD1 LEU A 638 8.265 −5.36614.549 1.00 25.02 ATOM 825 CD2 LEU A 638 8.740 −7.549 13.396 1.00 24.12ATOM 826 C LEU A 638 12.203 −5.348 11.543 1.00 26.64 ATOM 827 O LEU A638 13.301 −4.925 11.896 1.00 28.43 ATOM 828 N THR A 639 11.630 −5.01110.389 1.00 23.44 ATOM 829 CA THR A 639 12.253 −4.093 9.441 1.00 22.41ATOM 830 CB THR A 639 11.772 −4.343 8.004 1.00 28.95 ATOM 831 OG1 THR A639 10.378 −4.021 7.908 1.00 28.33 ATOM 832 CG2 THR A 639 11.982 −5.7947.611 1.00 28.40 ATOM 833 C THR A 639 11.870 −2.662 9.798 1.00 22.44ATOM 834 O THR A 639 10.921 −2.445 10.551 1.00 23.44 ATOM 835 N ASP A640 12.601 −1.695 9.250 1.00 24.48 ATOM 836 CA ASP A 640 12.321 −0.2889.508 1.00 24.67 ATOM 837 CB ASP A 640 13.313 0.604 8.747 1.00 30.57ATOM 838 CG ASP A 640 14.693 0.642 9.393 1.00 30.89 ATOM 839 OD1 ASP A640 15.634 1.146 8.743 1.00 30.85 ATOM 840 OD2 ASP A 640 14.838 0.18410.548 1.00 30.86 ATOM 841 C ASP A 640 10.895 0.038 9.074 1.00 24.64ATOM 842 O ASP A 640 10.177 0.761 9.765 1.00 24.23 ATOM 843 N LEU A 64110.491 −0.513 7.931 1.00 24.25 ATOM 844 CA LEU A 641 9.153 −0.291 7.3921.00 23.81 ATOM 845 CB LEU A 641 9.066 −0.863 5.975 1.00 25.82 ATOM 846CG LEU A 641 9.326 0.063 4.781 1.00 27.50 ATOM 847 CD1 LEU A 641 10.2671.188 5.137 1.00 25.96 ATOM 848 CD2 LEU A 641 9.858 −0.767 3.629 1.0026.21 ATOM 849 C LEU A 641 8.074 −0.914 8.269 1.00 23.08 ATOM 850 O LEUA 641 7.013 −0.332 8.464 1.00 24.13 ATOM 851 N GLU A 642 8.336 −2.1108.778 1.00 23.58 ATOM 852 CA GLU A 642 7.371 −2.771 9.639 1.00 24.03ATOM 853 CB GLU A 642 7.847 −4.188 9.966 1.00 29.79 ATOM 854 CG GLU A642 7.607 −5.150 8.816 1.00 30.52 ATOM 855 CD GLU A 642 8.276 −6.4929.004 1.00 30.88 ATOM 856 OE1 GLU A 642 7.928 −7.424 8.246 1.00 30.84ATOM 857 OE2 GLU A 642 9.147 −6.615 9.893 1.00 30.40 ATOM 858 C GLU A642 7.166 −1.947 10.911 1.00 24.17 ATOM 859 O GLU A 642 6.043 −1.81611.404 1.00 24.58 ATOM 860 N ILE A 643 8.260 −1.382 11.419 1.00 21.47ATOM 861 CA ILE A 643 8.230 −0.555 12.625 1.00 21.07 ATOM 862 CB ILE A643 9.659 −0.184 13.062 1.00 24.97 ATOM 863 CG2 ILE A 643 9.614 0.83314.195 1.00 23.30 ATOM 864 CG1 ILE A 643 10.409 −1.444 13.502 1.00 23.69ATOM 865 CD1 ILE A 643 11.900 −1.229 13.673 1.00 24.32 ATOM 866 C ILE A643 7.440 0.727 12.350 1.00 20.73 ATOM 867 O ILE A 643 6.536 1.08813.109 1.00 20.07 ATOM 868 N LEU A 644 7.792 1.405 11.259 1.00 21.45ATOM 869 CA LEU A 644 7.122 2.632 10.843 1.00 22.42 ATOM 870 CB LEU A644 7.707 3.112 9.510 1.00 22.90 ATOM 871 CG LEU A 644 7.028 4.294 8.8161.00 23.31 ATOM 872 CD1 LEU A 644 7.162 5.546 9.670 1.00 23.35 ATOM 873CD2 LEU A 644 7.671 4.506 7.449 1.00 22.87 ATOM 874 C LEU A 644 5.6232.400 10.686 1.00 22.48 ATOM 875 O LEU A 644 4.809 3.178 11.183 1.0021.76 ATOM 876 N ALA A 645 5.262 1.327 9.993 1.00 19.64 ATOM 877 CA ALAA 645 3.858 1.003 9.770 1.00 19.40 ATOM 878 CB ALA A 645 3.747 −0.1448.759 1.00 19.42 ATOM 879 C ALA A 645 3.110 0.643 11.062 1.00 18.96 ATOM880 O ALA A 645 1.946 1.016 11.238 1.00 16.29 ATOM 881 N LEU A 646 3.767−0.073 11.970 1.00 15.67 ATOM 882 CA LEU A 646 3.113 −0.458 13.218 1.0017.59 ATOM 883 CB LEU A 646 3.972 −1.464 13.982 1.00 21.09 ATOM 884 CGLEU A 646 4.011 −2.880 13.401 1.00 20.20 ATOM 885 CD1 LEU A 646 5.105−3.678 14.102 1.00 20.69 ATOM 886 CD2 LEU A 646 2.654 −3.552 13.561 1.0021.23 ATOM 887 C LEU A 646 2.826 0.750 14.112 1.00 16.19 ATOM 888 O LEUA 646 1.770 0.824 14.748 1.00 17.93 ATOM 889 N LEU A 647 3.767 1.68714.168 1.00 20.47 ATOM 890 CA LEU A 647 3.578 2.875 15.000 1.00 18.59ATOM 891 CB LEU A 647 4.874 3.682 15.097 1.00 19.99 ATOM 892 CG LEU A647 4.819 4.890 16.042 1.00 19.72 ATOM 893 CD1 LEU A 647 4.422 4.43217.445 1.00 21.01 ATOM 894 CD2 LEU A 647 6.168 5.563 16.078 1.00 21.38ATOM 895 C LEU A 647 2.447 3.735 14.436 1.00 19.57 ATOM 896 O LEU A 6471.583 4.199 15.183 1.00 19.14 ATOM 897 N ILE A 648 2.447 3.935 13.1201.00 17.04 ATOM 898 CA ILE A 648 1.393 4.714 12.475 1.00 16.34 ATOM 899CB ILE A 648 1.671 4.884 10.962 1.00 16.27 ATOM 900 CG2 ILE A 648 0.4285.441 10.251 1.00 17.73 ATOM 901 CG1 ILE A 648 2.895 5.787 10.770 1.0018.41 ATOM 902 CD1 ILE A 648 3.350 5.921 9.339 1.00 17.00 ATOM 903 C ILEA 648 0.060 3.999 12.674 1.00 17.17 ATOM 904 O ILE A 648 −0.946 4.62013.027 1.00 16.88 ATOM 905 N ALA A 649 0.056 2.684 12.477 1.00 17.97ATOM 906 CA ALA A 649 −1.171 1.912 12.634 1.00 18.14 ATOM 907 CB ALA A649 −0.927 0.460 12.228 1.00 19.75 ATOM 908 C ALA A 649 −1.724 1.97714.060 1.00 17.69 ATOM 909 O ALA A 649 −2.928 2.180 14.266 1.00 17.10ATOM 910 N ALA A 650 −0.850 1.802 15.047 1.00 16.14 ATOM 911 CA ALA A650 −1.276 1.846 16.438 1.00 15.98 ATOM 912 CB ALA A 650 −0.070 1.70317.365 1.00 18.40 ATOM 913 C ALA A 650 −1.987 3.175 16.708 1.00 16.55ATOM 914 O ALA A 650 −3.049 3.214 17.327 1.00 17.85 ATOM 915 N LEU A 651−1.401 4.259 16.226 1.00 17.09 ATOM 916 CA LEU A 651 −1.974 5.589 16.4381.00 17.07 ATOM 917 CB LEU A 651 −0.956 6.659 16.056 1.00 20.77 ATOM 918CG LEU A 651 0.304 6.766 16.906 1.00 20.44 ATOM 919 CD1 LEU A 651 1.3267.596 16.156 1.00 20.57 ATOM 920 CD2 LEU A 651 −0.036 7.402 18.255 1.0020.14 ATOM 921 C LEU A 651 −3.246 5.846 15.648 1.00 17.89 ATOM 922 O LEUA 651 −4.133 6.569 16.102 1.00 17.40 ATOM 923 N SER A 652 −3.335 5.24814.465 1.00 14.66 ATOM 924 CA SER A 652 −4.484 5.470 13.591 1.00 16.84ATOM 925 CB SER A 652 −4.013 5.620 12.141 1.00 19.10 ATOM 926 OG SER A652 −2.948 6.535 12.014 1.00 18.78 ATOM 927 C SER A 652 −5.549 4.38613.596 1.00 17.02 ATOM 928 O SER A 652 −6.593 4.574 12.987 1.00 16.48ATOM 929 N HIS A 653 −5.302 3.280 14.292 1.00 19.51 ATOM 930 CA HIS A653 −6.219 2.143 14.241 1.00 18.51 ATOM 931 CB HIS A 653 −5.607 0.93914.972 1.00 15.82 ATOM 932 CG HIS A 653 −5.944 0.882 16.427 1.00 16.43ATOM 933 CD2 HIS A 653 −6.947 0.252 17.079 1.00 15.65 ATOM 934 ND1 HIS A653 −5.237 1.574 17.385 1.00 14.87 ATOM 935 CE1 HIS A 653 −5.794 1.37618.567 1.00 15.10 ATOM 936 NE2 HIS A 653 −6.838 0.580 18.406 1.00 15.73ATOM 937 C HIS A 653 −7.681 2.284 14.652 1.00 19.28 ATOM 938 O HIS A 653−8.486 1.441 14.289 1.00 17.55 ATOM 939 N ASP A 654 −8.039 3.329 15.3951.00 14.03 ATOM 940 CA ASP A 654 −9.434 3.505 15.811 1.00 13.68 ATOM 941CB ASP A 654 −9.576 3.404 17.342 1.00 17.23 ATOM 942 CG ASP A 654 −9.8931.995 17.816 1.00 16.81 ATOM 943 OD1 ASP A 654 −10.559 1.251 17.063 1.0016.45 ATOM 944 OD2 ASP A 654 −9.510 1.647 18.953 1.00 16.54 ATOM 945 CASP A 654 −9.986 4.858 15.351 1.00 14.35 ATOM 946 O ASP A 654 −11.0045.325 15.870 1.00 15.00 ATOM 947 N LEU A 655 −9.342 5.461 14.353 1.0014.26 ATOM 948 CA LEU A 655 −9.745 6.777 13.838 1.00 15.05 ATOM 949 CBLEU A 655 −8.976 7.071 12.542 1.00 21.81 ATOM 950 CG LEU A 655 −8.0288.263 12.357 1.00 25.53 ATOM 951 CD1 LEU A 655 −7.712 8.958 13.671 1.0022.91 ATOM 952 CD2 LEU A 655 −6.766 7.763 11.665 1.00 22.84 ATOM 953 CLEU A 655 −11.257 6.941 13.591 1.00 16.32 ATOM 954 O LEU A 655 −11.8896.120 12.923 1.00 15.44 ATOM 955 N ASP A 656 −11.826 8.013 14.147 1.0016.42 ATOM 956 CA ASP A 656 −13.251 8.326 13.988 1.00 17.71 ATOM 957 CBASP A 656 −13.556 8.647 12.508 1.00 20.19 ATOM 958 CG ASP A 656 −14.9059.353 12.312 1.00 20.24 ATOM 959 OD1 ASP A 656 −15.243 10.252 13.1101.00 19.07 ATOM 960 OD2 ASP A 656 −15.623 9.021 11.344 1.00 19.47 ATOM961 C ASP A 656 −14.197 7.232 14.496 1.00 16.50 ATOM 962 O ASP A 656−15.295 7.060 13.971 1.00 16.42 ATOM 963 N HIS A 657 −13.777 6.50215.523 1.00 16.01 ATOM 964 CA HIS A 657 −14.627 5.454 16.073 1.00 15.64ATOM 965 CB HIS A 657 −13.902 4.710 17.196 1.00 18.44 ATOM 966 CG HIS A657 −14.585 3.446 17.606 1.00 19.68 ATOM 967 CD2 HIS A 657 −15.832 3.22418.080 1.00 15.96 ATOM 968 ND1 HIS A 657 −13.979 2.209 17.524 1.00 19.05ATOM 969 CE1 HIS A 657 −14.825 1.281 17.930 1.00 16.34 ATOM 970 NE2 HISA 657 −15.958 1.871 18.271 1.00 21.05 ATOM 971 C HIS A 657 −15.893 6.12616.611 1.00 17.49 ATOM 972 O HIS A 657 −15.826 7.093 17.377 1.00 16.58ATOM 973 N PRO A 658 −17.068 5.625 16.216 1.00 19.29 ATOM 974 CD PRO A658 −17.281 4.579 15.199 1.00 17.12 ATOM 975 CA PRO A 658 −18.346 6.18916.659 1.00 19.86 ATOM 976 CB PRO A 658 −19.313 5.701 15.595 1.00 16.51ATOM 977 CG PRO A 658 −18.772 4.311 15.313 1.00 15.25 ATOM 978 C PRO A658 −18.789 5.780 18.058 1.00 19.74 ATOM 979 O PRO A 658 −19.745 6.33518.589 1.00 20.03 ATOM 980 N GLY A 659 −18.125 4.788 18.639 1.00 16.93ATOM 981 CA GLY A 659 −18.500 4.360 19.972 1.00 18.25 ATOM 982 C GLY A659 −19.458 3.189 20.003 1.00 18.14 ATOM 983 O GLY A 659 −19.993 2.85721.060 1.00 17.96 ATOM 984 N VAL A 660 −19.695 2.581 18.844 1.00 19.22ATOM 985 CA VAL A 660 −20.573 1.418 18.749 1.00 20.26 ATOM 986 CB VAL A660 −21.909 1.771 18.060 1.00 19.84 ATOM 987 CG1 VAL A 660 −22.697 2.73018.941 1.00 20.64 ATOM 988 CG2 VAL A 660 −21.655 2.391 16.698 1.00 20.17ATOM 989 C VAL A 660 −19.844 0.334 17.958 1.00 20.35 ATOM 990 O VAL A660 −18.953 0.630 17.160 1.00 20.64 ATOM 991 N SER A 661 −20.226 −0.91518.190 1.00 18.66 ATOM 992 CA SER A 661 −19.605 −2.069 17.541 1.00 19.40ATOM 993 CB SER A 661 −20.001 −3.341 18.278 1.00 23.46 ATOM 994 OG SER A661 −21.369 −3.622 18.044 1.00 22.76 ATOM 995 C SER A 661 −19.955 −2.26016.069 1.00 19.19 ATOM 996 O SER A 661 −20.857 −1.614 15.539 1.00 19.47ATOM 997 N ASN A 662 −19.237 −3.175 15.421 1.00 20.96 ATOM 998 CA ASN A662 −19.493 −3.489 14.018 1.00 21.17 ATOM 999 CB ASN A 662 −18.474−4.500 13.487 1.00 20.86 ATOM 1000 CG ASN A 662 −17.189 −3.844 13.0531.00 20.37 ATOM 1001 OD1 ASN A 662 −17.200 −2.702 12.606 1.00 21.25 ATOM1002 ND2 ASN A 662 −16.078 −4.566 13.158 1.00 19.75 ATOM 1003 C ASN A662 −20.894 −4.065 13.895 1.00 21.10 ATOM 1004 O ASN A 662 −21.651−3.713 12.985 1.00 21.05 ATOM 1005 N GLN A 663 −21.242 −4.941 14.8311.00 25.13 ATOM 1006 CA GLN A 663 −22.556 −5.555 14.836 1.00 26.08 ATOM1007 CB GLN A 663 −22.696 −6.503 16.031 1.00 35.28 ATOM 1008 CG GLN A663 −21.884 −7.790 15.904 1.00 36.63 ATOM 1009 CD GLN A 663 −20.381−7.582 16.043 1.00 36.48 ATOM 1010 OE1 GLN A 663 −19.588 −8.447 15.6651.00 36.95 ATOM 1011 NE2 GLN A 663 −19.983 −6.441 16.600 1.00 36.26 ATOM1012 C GLN A 663 −23.638 −4.480 14.881 1.00 25.84 ATOM 1013 O GLN A 663−24.625 −4.554 14.153 1.00 25.82 ATOM 1014 N PHE A 664 −23.451 −3.47415.730 1.00 24.41 ATOM 1015 CA PHE A 664 −24.423 −2.394 15.832 1.0025.34 ATOM 1016 CB PHE A 664 −23.991 −1.391 16.906 1.00 26.39 ATOM 1017CG PHE A 664 −24.932 −0.226 17.069 1.00 27.42 ATOM 1018 CD1 PHE A 664−24.841 0.881 16.230 1.00 26.41 ATOM 1019 CD2 PHE A 664 −25.915 −0.24018.057 1.00 27.03 ATOM 1020 CE1 PHE A 664 −25.713 1.963 16.367 1.0027.10 ATOM 1021 CE2 PHE A 664 −26.795 0.840 18.202 1.00 27.63 ATOM 1022CZ PHE A 664 −26.687 1.943 17.350 1.00 26.59 ATOM 1023 C PHE A 664−24.577 −1.697 14.476 1.00 25.16 ATOM 1024 O PHE A 664 −25.691 −1.48514.006 1.00 24.58 ATOM 1025 N LEU A 665 −23.454 −1.361 13.847 1.00 21.05ATOM 1026 CA LEU A 665 −23.479 −0.698 12.542 1.00 22.93 ATOM 1027 CB LEUA 665 −22.058 −0.348 12.104 1.00 22.29 ATOM 1028 CG LEU A 665 −21.3280.745 12.893 1.00 22.66 ATOM 1029 CD1 LEU A 665 −19.914 0.890 12.3471.00 22.68 ATOM 1030 CD2 LEU A 665 −22.069 2.064 12.776 1.00 22.45 ATOM1031 C LEU A 665 −24.147 −1.563 11.471 1.00 22.68 ATOM 1032 O LEU A 665−24.748 −1.053 10.520 1.00 23.83 ATOM 1033 N ILE A 666 −24.031 −2.87411.618 1.00 24.12 ATOM 1034 CA ILE A 666 −24.635 −3.794 10.664 1.0024.57 ATOM 1035 CB ILE A 666 −24.023 −5.204 10.785 1.00 26.67 ATOM 1036CG2 ILE A 666 −24.819 −6.195 9.951 1.00 26.86 ATOM 1037 CG1 ILE A 666−22.559 −5.176 10.340 1.00 25.51 ATOM 1038 CD1 ILE A 666 −21.811 −6.48310.553 1.00 26.41 ATOM 1039 C ILE A 666 −26.136 −3.880 10.926 1.00 26.29ATOM 1040 O ILE A 666 −26.937 −3.859 9.993 1.00 26.10 ATOM 1041 N ASN A667 −26.511 −3.968 12.197 1.00 31.89 ATOM 1042 CA ASN A 667 −27.920−4.070 12.563 1.00 34.09 ATOM 1043 CB ASN A 667 −28.063 −4.437 14.0441.00 34.18 ATOM 1044 CG ASN A 667 −27.511 −5.809 14.355 1.00 33.95 ATOM1045 OD1 ASN A 667 −27.608 −6.722 13.538 1.00 34.50 ATOM 1046 ND2 ASN A667 −26.939 −5.969 15.544 1.00 34.36 ATOM 1047 C ASN A 667 −28.733−2.816 12.270 1.00 34.67 ATOM 1048 O ASN A 667 −29.944 −2.891 12.0581.00 34.88 ATOM 1049 N THR A 668 −28.073 −1.665 12.264 1.00 41.41 ATOM1050 CA THR A 668 −28.755 −0.408 11.993 1.00 41.66 ATOM 1051 CB THR A668 −28.180 0.728 12.851 1.00 34.82 ATOM 1052 OG1 THR A 668 −26.7740.855 12.598 1.00 34.37 ATOM 1053 CG2 THR A 668 −28.404 0.438 14.3251.00 34.77 ATOM 1054 C THR A 668 −28.630 −0.028 10.521 1.00 41.72 ATOM1055 O THR A 668 −29.012 1.070 10.121 1.00 42.66 ATOM 1056 N ASN A 669−28.096 −0.945 9.720 1.00 36.50 ATOM 1057 CA ASN A 669 −27.916 −0.7158.289 1.00 35.43 ATOM 1058 CB ASN A 669 −29.271 −0.756 7.581 1.00 39.66ATOM 1059 CG ASN A 669 −29.861 −2.147 7.553 1.00 39.15 ATOM 1060 OD1 ASNA 669 −29.314 −3.048 6.919 1.00 39.61 ATOM 1061 ND2 ASN A 669 −30.974−2.334 8.247 1.00 39.97 ATOM 1062 C ASN A 669 −27.217 0.603 8.002 1.0033.95 ATOM 1063 O ASN A 669 −27.676 1.406 7.187 1.00 35.22 ATOM 1064 NSER A 670 −26.098 0.816 8.684 1.00 24.12 ATOM 1065 CA SER A 670 −25.3042.020 8.524 1.00 24.45 ATOM 1066 CB SER A 670 −24.162 2.032 9.543 1.0036.85 ATOM 1067 OG SER A 670 −23.245 3.081 9.279 1.00 38.12 ATOM 1068 CSER A 670 −24.727 2.056 7.120 1.00 22.19 ATOM 1069 O SER A 670 −24.5291.013 6.498 1.00 22.80 ATOM 1070 N GLU A 671 −24.461 3.261 6.626 1.0025.15 ATOM 1071 CA GLU A 671 −23.888 3.426 5.299 1.00 25.09 ATOM 1072 CBGLU A 671 −23.736 4.911 4.975 1.00 30.03 ATOM 1073 CG GLU A 671 −23.3225.198 3.547 1.00 30.00 ATOM 1074 CD GLU A 671 −23.174 6.683 3.277 1.0030.78 ATOM 1075 OE1 GLU A 671 −22.113 7.253 3.613 1.00 30.04 ATOM 1076OE2 GLU A 671 −24.132 7.283 2.742 1.00 30.29 ATOM 1077 C GLU A 671−22.521 2.757 5.281 1.00 23.99 ATOM 1078 O GLU A 671 −22.087 2.222 4.2671.00 24.80 ATOM 1079 N LEU A 672 −21.857 2.786 6.429 1.00 23.33 ATOM1080 CA LEU A 672 −20.533 2.196 6.581 1.00 21.52 ATOM 1081 CB LEU A 672−20.010 2.512 7.984 1.00 30.40 ATOM 1082 CG LEU A 672 −18.683 3.2608.158 1.00 31.15 ATOM 1083 CD1 LEU A 672 −18.555 4.398 7.164 1.00 30.73ATOM 1084 CD2 LEU A 672 −18.603 3.772 9.586 1.00 31.17 ATOM 1085 C LEU A672 −20.561 0.685 6.349 1.00 22.19 ATOM 1086 O LEU A 672 −19.688 0.1385.673 1.00 20.56 ATOM 1087 N ALA A 673 −21.565 0.014 6.910 1.00 20.08ATOM 1088 CA ALA A 673 −21.685 −1.434 6.766 1.00 20.23 ATOM 1089 CB ALAA 673 −22.827 −1.958 7.639 1.00 23.81 ATOM 1090 C ALA A 673 −21.934−1.794 5.310 1.00 20.27 ATOM 1091 O ALA A 673 −21.446 −2.808 4.821 1.0020.29 ATOM 1092 N LEU A 674 −22.714 −0.970 4.620 1.00 18.83 ATOM 1093 CALEU A 674 −22.998 −1.229 3.213 1.00 20.25 ATOM 1094 CB LEU A 674 −24.063−0.265 2.694 1.00 26.85 ATOM 1095 CG LEU A 674 −24.330 −0.385 1.189 1.0027.73 ATOM 1096 CD1 LEU A 674 −24.803 −1.793 0.849 1.00 27.05 ATOM 1097CD2 LEU A 674 −25.364 0.646 0.779 1.00 27.39 ATOM 1098 C LEU A 674−21.740 −1.082 2.363 1.00 18.25 ATOM 1099 O LEU A 674 −21.454 −1.9151.500 1.00 21.42 ATOM 1100 N MET A 675 −20.980 −0.027 2.624 1.00 22.09ATOM 1101 CA MET A 675 −19.758 0.244 1.874 1.00 23.03 ATOM 1102 CB MET A675 −19.140 1.562 2.330 1.00 41.71 ATOM 1103 CG MET A 675 −20.013 2.7712.096 1.00 42.43 ATOM 1104 SD MET A 675 −19.158 4.258 2.607 1.00 43.58ATOM 1105 CE MET A 675 −18.192 4.598 1.138 1.00 42.87 ATOM 1106 C MET A675 −18.711 −0.848 2.018 1.00 23.59 ATOM 1107 O MET A 675 −17.961 −1.1301.079 1.00 22.39 ATOM 1108 N TYR A 676 −18.662 −1.463 3.193 1.00 22.64ATOM 1109 CA TYR A 676 −17.670 −2.495 3.451 1.00 22.20 ATOM 1110 CB TYRA 676 −16.894 −2.113 4.717 1.00 21.16 ATOM 1111 CG TYR A 676 −16.197−0.767 4.574 1.00 21.36 ATOM 1112 CD1 TYR A 676 −16.385 0.249 5.513 1.0021.19 ATOM 1113 CE1 TYR A 676 −15.774 1.501 5.352 1.00 20.94 ATOM 1114CD2 TYR A 676 −15.378 −0.503 3.475 1.00 20.92 ATOM 1115 CE2 TYR A 676−14.760 0.739 3.307 1.00 20.99 ATOM 1116 CZ TYR A 676 −14.964 1.7344.242 1.00 21.41 ATOM 1117 OH TYR A 676 −14.374 2.969 4.059 1.00 22.70ATOM 1118 C TYR A 676 −18.206 −3.926 3.531 1.00 23.64 ATOM 1119 O TYR A676 −17.519 −4.824 4.019 1.00 22.37 ATOM 1120 N ASN A 677 −19.421 −4.1293.025 1.00 21.83 ATOM 1121 CA ASN A 677 −20.071 −5.444 2.995 1.00 23.13ATOM 1122 CB ASN A 677 −19.487 −6.296 1.861 1.00 56.74 ATOM 1123 CG ASNA 677 −18.007 −6.571 2.033 1.00 57.80 ATOM 1124 OD1 ASN A 677 −17.594−7.241 2.979 1.00 58.17 ATOM 1125 ND2 ASN A 677 −17.197 −6.052 1.1161.00 58.15 ATOM 1126 C ASN A 677 −20.019 −6.223 4.311 1.00 22.92 ATOM1127 O ASN A 677 −19.726 −7.425 4.332 1.00 22.51 ATOM 1128 N ASP A 678−20.317 −5.521 5.398 1.00 22.36 ATOM 1129 CA ASP A 678 −20.353 −6.0966.742 1.00 23.31 ATOM 1130 CB ASP A 678 −21.461 −7.146 6.843 1.00 24.85ATOM 1131 CG ASP A 678 −22.824 −6.604 6.466 1.00 25.27 ATOM 1132 OD1 ASPA 678 −23.031 −5.376 6.536 1.00 23.89 ATOM 1133 OD2 ASP A 678 −23.699−7.420 6.111 1.00 26.42 ATOM 1134 C ASP A 678 −19.070 −6.725 7.261 1.0021.81 ATOM 1135 O ASP A 678 −19.084 −7.336 8.332 1.00 23.49 ATOM 1136 NGLU A 679 −17.972 −6.578 6.533 1.00 19.14 ATOM 1137 CA GLU A 679 −16.703−7.166 6.962 1.00 20.71 ATOM 1138 CB GLU A 679 −15.988 −7.819 5.778 1.0046.03 ATOM 1139 CG GLU A 679 −16.640 −9.084 5.259 1.00 47.01 ATOM 1140CD GLU A 679 −15.840 −9.724 4.139 1.00 47.28 ATOM 1141 OE1 GLU A 679−15.723 −9.106 3.059 1.00 47.36 ATOM 1142 OE2 GLU A 679 −15.320 −10.8414.337 1.00 47.19 ATOM 1143 C GLU A 679 −15.770 −6.137 7.582 1.00 19.51ATOM 1144 O GLU A 679 −15.378 −5.185 6.912 1.00 20.45 ATOM 1145 N SER A680 −15.407 −6.345 8.848 1.00 17.83 ATOM 1146 CA SER A 680 −14.505−5.442 9.574 1.00 17.23 ATOM 1147 CB SER A 680 −13.043 −5.747 9.224 1.0021.15 ATOM 1148 OG SER A 680 −12.707 −7.098 9.511 1.00 20.61 ATOM 1149 CSER A 680 −14.827 −3.997 9.202 1.00 16.25 ATOM 1150 O SER A 680 −13.941−3.218 8.844 1.00 15.64 ATOM 1151 N VAL A 681 −16.108 −3.664 9.309 1.0018.34 ATOM 1152 CA VAL A 681 −16.629 −2.353 8.947 1.00 16.30 ATOM 1153CB VAL A 681 −18.115 −2.245 9.327 1.00 19.28 ATOM 1154 CG1 VAL A 681−18.674 −0.895 8.881 1.00 20.72 ATOM 1155 CG2 VAL A 681 −18.894 −3.3978.665 1.00 19.24 ATOM 1156 C VAL A 681 −15.864 −1.173 9.529 1.00 16.04ATOM 1157 O VAL A 681 −15.356 −0.347 8.790 1.00 17.05 ATOM 1158 N LEU A681A −15.782 −1.110 10.852 1.00 15.07 ATOM 1159 CA LEU A 681A −15.079−0.028 11.529 1.00 16.07 ATOM 1160 CB LEU A 681A −15.166 −0.217 13.0431.00 22.39 ATOM 1161 CG LEU A 681A −16.520 0.073 13.680 1.00 24.40 ATOM1162 CD1 LEU A 681A −16.571 −0.536 15.076 1.00 24.68 ATOM 1163 CD2 LEU A681A −16.732 1.573 13.710 1.00 25.32 ATOM 1164 C LEU A 681A −13.6130.027 11.125 1.00 15.73 ATOM 1165 O LEU A 681A −13.070 1.089 10.848 1.0014.66 ATOM 1166 N GLU A 682 −12.975 −1.134 11.078 1.00 14.20 ATOM 1167CA GLU A 682 −11.566 −1.181 10.731 1.00 16.26 ATOM 1168 CB GLU A 682−11.042 −2.601 10.954 1.00 17.70 ATOM 1169 CG GLU A 682 −11.075 −3.04312.424 1.00 17.27 ATOM 1170 CD GLU A 682 −12.466 −3.381 12.956 1.0017.63 ATOM 1171 OE1 GLU A 682 −13.350 −3.778 12.164 1.00 16.51 ATOM 1172OE2 GLU A 682 −12.672 −3.273 14.192 1.00 18.25 ATOM 1173 C GLU A 682−11.272 −0.675 9.313 1.00 13.40 ATOM 1174 O GLU A 682 −10.257 −0.0109.088 1.00 16.15 ATOM 1175 N HIS A 683 −12.140 −0.983 8.353 1.00 14.40ATOM 1176 CA HIS A 683 −11.943 −0.474 7.001 1.00 15.72 ATOM 1177 CB HISA 683 −12.955 −1.084 6.030 1.00 20.22 ATOM 1178 CG HIS A 683 −12.527−2.406 5.483 1.00 21.36 ATOM 1179 CD2 HIS A 683 −12.905 −3.667 5.8001.00 22.11 ATOM 1180 ND1 HIS A 683 −11.538 −2.529 4.531 1.00 19.70 ATOM1181 CE1 HIS A 683 −11.325 −3.810 4.286 1.00 20.00 ATOM 1182 NE2 HIS A683 −12.139 −4.520 5.044 1.00 21.26 ATOM 1183 C HIS A 683 −12.102 1.0467.044 1.00 15.07 ATOM 1184 O HIS A 683 −11.395 1.772 6.343 1.00 16.13ATOM 1185 N HIS A 684 −13.033 1.519 7.874 1.00 16.25 ATOM 1186 CA HIS A684 −13.258 2.952 8.026 1.00 17.73 ATOM 1187 CB HIS A 684 −14.505 3.2168.878 1.00 19.40 ATOM 1188 CG HIS A 684 −14.776 4.670 9.116 1.00 20.37ATOM 1189 CD2 HIS A 684 −14.870 5.387 10.261 1.00 19.50 ATOM 1190 ND1HIS A 684 −14.982 5.563 8.087 1.00 20.04 ATOM 1191 CE1 HIS A 684 −15.1946.766 8.588 1.00 19.05 ATOM 1192 NE2 HIS A 684 −15.131 6.688 9.903 1.0018.64 ATOM 1193 C HIS A 684 −12.038 3.601 8.677 1.00 17.41 ATOM 1194 OHIS A 684 −11.602 4.677 8.248 1.00 17.52 ATOM 1195 N HIS A 685 −11.4912.952 9.704 1.00 16.56 ATOM 1196 CA HIS A 685 −10.316 3.481 10.387 1.0017.88 ATOM 1197 CB HIS A 685 −9.886 2.568 11.553 1.00 17.97 ATOM 1198 CGHIS A 685 −10.943 2.365 12.599 1.00 17.64 ATOM 1199 CD2 HIS A 685−11.311 1.258 13.291 1.00 17.69 ATOM 1200 ND1 HIS A 685 −11.728 3.39213.079 1.00 16.45 ATOM 1201 CE1 HIS A 685 −12.533 2.927 14.020 1.0018.14 ATOM 1202 NE2 HIS A 685 −12.299 1.634 14.168 1.00 17.23 ATOM 1203C HIS A 685 −9.178 3.619 9.380 1.00 17.11 ATOM 1204 O HIS A 685 −8.4824.639 9.348 1.00 17.09 ATOM 1205 N PHE A 686 −8.984 2.596 8.551 1.0017.41 ATOM 1206 CA PHE A 686 −7.928 2.656 7.551 1.00 17.43 ATOM 1207 CBPHE A 686 −7.766 1.325 6.810 1.00 22.00 ATOM 1208 CG PHE A 686 −6.7381.384 5.715 1.00 21.91 ATOM 1209 CD1 PHE A 686 −5.396 1.591 6.014 1.0022.44 ATOM 1210 CD2 PHE A 686 −7.123 1.328 4.379 1.00 22.63 ATOM 1211CE1 PHE A 686 −4.449 1.754 4.998 1.00 21.95 ATOM 1212 CE2 PHE A 686−6.186 1.487 3.356 1.00 22.74 ATOM 1213 CZ PHE A 686 −4.847 1.704 3.6681.00 23.18 ATOM 1214 C PHE A 686 −8.183 3.760 6.531 1.00 18.51 ATOM 1215O PHE A 686 −7.250 4.436 6.104 1.00 18.35 ATOM 1216 N ASP A 687 −9.4393.934 6.130 1.00 17.80 ATOM 1217 CA ASP A 687 −9.768 4.974 5.166 1.0018.73 ATOM 1218 CB ASP A 687 −11.262 4.969 4.836 1.00 27.45 ATOM 1219 CGASP A 687 −11.661 6.129 3.932 1.00 29.42 ATOM 1220 OD1 ASP A 687 −11.1626.190 2.789 1.00 29.29 ATOM 1221 OD2 ASP A 687 −12.465 6.984 4.366 1.0029.84 ATOM 1222 C ASP A 687 −9.389 6.329 5.751 1.00 17.84 ATOM 1223 OASP A 687 −8.793 7.164 5.070 1.00 18.06 ATOM 1224 N GLN A 688 −9.7266.534 7.020 1.00 20.35 ATOM 1225 CA GLN A 688 −9.412 7.786 7.703 1.0019.96 ATOM 1226 CB GLN A 688 −10.060 7.804 9.085 1.00 24.85 ATOM 1227 CGGLN A 688 −11.577 7.795 9.021 1.00 25.62 ATOM 1228 CD GLN A 688 −12.1209.081 8.440 1.00 26.01 ATOM 1229 OE1 GLN A 688 −12.052 10.129 9.076 1.0027.97 ATOM 1230 NE2 GLN A 688 −12.647 9.012 7.221 1.00 27.26 ATOM 1231 CGLN A 688 −7.911 7.969 7.831 1.00 20.01 ATOM 1232 O GLN A 688 −7.4069.077 7.689 1.00 19.66 ATOM 1233 N CYS A 689 −7.202 6.871 8.091 1.0018.42 ATOM 1234 CA CYS A 689 −5.746 6.902 8.229 1.00 18.66 ATOM 1235 CBCYS A 689 −5.224 5.498 8.556 1.00 19.50 ATOM 1236 SG CYS A 689 −3.4255.370 8.637 1.00 16.97 ATOM 1237 C CYS A 689 −5.098 7.413 6.942 1.0018.50 ATOM 1238 O CYS A 689 −4.234 8.295 6.977 1.00 19.39 ATOM 1239 NLEU A 690 −5.524 6.854 5.812 1.00 19.82 ATOM 1240 CA LEU A 690 −5.0067.235 4.497 1.00 20.55 ATOM 1241 CB LEU A 690 −5.556 6.288 3.429 1.0025.80 ATOM 1242 CG LEU A 690 −4.985 6.446 2.017 1.00 26.79 ATOM 1243 CD1LEU A 690 −3.507 6.105 2.029 1.00 27.37 ATOM 1244 CD2 LEU A 690 −5.7285.535 1.059 1.00 27.51 ATOM 1245 C LEU A 690 −5.389 8.678 4.148 1.0019.76 ATOM 1246 O LEU A 690 −4.621 9.401 3.521 1.00 21.37 ATOM 1247 NMET A 691 −6.587 9.088 4.549 1.00 21.76 ATOM 1248 CA MET A 691 −7.04410.451 4.285 1.00 21.56 ATOM 1249 CB MET A 691 −8.450 10.654 4.851 1.0039.93 ATOM 1250 CG MET A 691 −9.006 12.052 4.633 1.00 40.74 ATOM 1251 SDMET A 691 −10.617 12.278 5.400 1.00 42.16 ATOM 1252 CE MET A 691 −10.13812.715 7.088 1.00 40.97 ATOM 1253 C MET A 691 −6.079 11.451 4.928 1.0022.42 ATOM 1254 O MET A 691 −5.673 12.435 4.300 1.00 21.69 ATOM 1255 NILE A 692 −5.712 11.200 6.179 1.00 20.61 ATOM 1256 CA ILE A 692 −4.79912.094 6.878 1.00 21.43 ATOM 1257 CB ILE A 692 −4.704 11.744 8.385 1.0023.64 ATOM 1258 CG2 ILE A 692 −3.670 12.633 9.066 1.00 23.04 ATOM 1259CG1 ILE A 692 −6.072 11.921 9.056 1.00 23.49 ATOM 1260 CD1 ILE A 692−6.591 13.352 9.054 1.00 25.57 ATOM 1261 C ILE A 692 −3.403 12.045 6.2521.00 22.50 ATOM 1262 O ILE A 692 −2.759 13.081 6.084 1.00 22.01 ATOM1263 N LEU A 693 −2.940 10.846 5.901 1.00 24.42 ATOM 1264 CA LEU A 693−1.615 10.689 5.298 1.00 25.47 ATOM 1265 CB LEU A 693 −1.288 9.203 5.0871.00 21.69 ATOM 1266 CG LEU A 693 −0.950 8.368 6.333 1.00 21.16 ATOM1267 CD1 LEU A 693 −0.945 6.888 5.985 1.00 22.43 ATOM 1268 CD2 LEU A 6930.411 8.794 6.887 1.00 21.71 ATOM 1269 C LEU A 693 −1.499 11.437 3.9721.00 25.25 ATOM 1270 O LEU A 693 −0.414 11.883 3.601 1.00 26.01 ATOM1271 N ASN A 694 −2.614 11.579 3.261 1.00 23.58 ATOM 1272 CA ASN A 694−2.610 12.284 1.981 1.00 22.99 ATOM 1273 CB ASN A 694 −3.613 11.6561.005 1.00 26.66 ATOM 1274 CG ASN A 694 −3.178 10.294 0.514 1.00 26.69ATOM 1275 OD1 ASN A 694 −2.009 10.078 0.209 1.00 27.10 ATOM 1276 ND2 ASNA 694 −4.127 9.369 0.413 1.00 27.29 ATOM 1277 C ASN A 694 −2.949 13.7632.132 1.00 23.59 ATOM 1278 O ASN A 694 −2.913 14.508 1.155 1.00 24.38ATOM 1279 N SER A 695 −3.285 14.181 3.348 1.00 24.35 ATOM 1280 CA SER A695 −3.644 15.572 3.596 1.00 24.87 ATOM 1281 CB SER A 695 −4.279 15.7274.980 1.00 30.85 ATOM 1282 OG SER A 695 −5.570 15.146 5.009 1.00 31.53ATOM 1283 C SER A 695 −2.431 16.475 3.496 1.00 25.45 ATOM 1284 O SER A695 −1.399 16.213 4.108 1.00 25.07 ATOM 1285 N PRO A 696 −2.544 17.5582.717 1.00 28.09 ATOM 1286 CD PRO A 696 −3.728 18.069 2.009 1.00 32.92ATOM 1287 CA PRO A 696 −1.410 18.471 2.579 1.00 28.93 ATOM 1288 CB PRO A696 −1.978 19.603 1.718 1.00 32.61 ATOM 1289 CG PRO A 696 −3.460 19.5521.991 1.00 33.55 ATOM 1290 C PRO A 696 −0.900 18.944 3.940 1.00 28.17ATOM 1291 O PRO A 696 −1.686 19.310 4.818 1.00 27.52 ATOM 1292 N GLY A697 0.419 18.913 4.104 1.00 27.38 ATOM 1293 CA GLY A 697 1.035 19.3365.347 1.00 27.26 ATOM 1294 C GLY A 697 1.106 18.239 6.391 1.00 27.36ATOM 1295 O GLY A 697 1.688 18.430 7.460 1.00 27.28 ATOM 1296 N ASN A698 0.523 17.084 6.080 1.00 24.05 ATOM 1297 CA ASN A 698 0.506 15.9517.006 1.00 24.41 ATOM 1298 CB ASN A 698 −0.937 15.592 7.379 1.00 26.46ATOM 1299 CG ASN A 698 −1.624 16.668 8.190 1.00 26.12 ATOM 1300 OD1 ASNA 698 −2.038 17.702 7.664 1.00 27.64 ATOM 1301 ND2 ASN A 698 −1.74916.428 9.486 1.00 26.42 ATOM 1302 C ASN A 698 1.165 14.698 6.436 1.0024.62 ATOM 1303 O ASN A 698 1.157 13.643 7.076 1.00 22.80 ATOM 1304 NGLN A 699 1.734 14.812 5.240 1.00 24.05 ATOM 1305 CA GLN A 699 2.34813.669 4.572 1.00 24.71 ATOM 1306 CB GLN A 699 2.486 13.982 3.083 1.0037.81 ATOM 1307 CG GLN A 699 1.165 14.399 2.451 1.00 38.52 ATOM 1308 CDGLN A 699 1.324 14.910 1.036 1.00 38.73 ATOM 1309 OE1 GLN A 699 1.76814.184 0.148 1.00 39.77 ATOM 1310 NE2 GLN A 699 0.964 16.170 0.819 1.0038.87 ATOM 1311 C GLN A 699 3.687 13.229 5.151 1.00 23.74 ATOM 1312 OGLN A 699 4.739 13.494 4.573 1.00 24.82 ATOM 1313 N ILE A 700 3.63912.530 6.284 1.00 23.85 ATOM 1314 CA ILE A 700 4.853 12.058 6.938 1.0023.88 ATOM 1315 CB ILE A 700 4.572 11.572 8.374 1.00 25.21 ATOM 1316 CG2ILE A 700 4.101 12.736 9.225 1.00 24.98 ATOM 1317 CG1 ILE A 700 3.52810.454 8.363 1.00 25.64 ATOM 1318 CD1 ILE A 700 3.370 9.764 9.699 1.0025.16 ATOM 1319 C ILE A 700 5.550 10.935 6.182 1.00 24.95 ATOM 1320 OILE A 700 6.662 10.540 6.546 1.00 24.94 ATOM 1321 N LEU A 701 4.90410.426 5.135 1.00 25.36 ATOM 1322 CA LEU A 701 5.476 9.350 4.327 1.0025.43 ATOM 1323 CB LEU A 701 4.460 8.218 4.146 1.00 25.64 ATOM 1324 CGLEU A 701 3.976 7.487 5.401 1.00 25.01 ATOM 1325 CD1 LEU A 701 2.9756.403 5.008 1.00 25.21 ATOM 1326 CD2 LEU A 701 5.161 6.879 6.124 1.0025.48 ATOM 1327 C LEU A 701 5.904 9.859 2.951 1.00 27.13 ATOM 1328 O LEUA 701 6.280 9.075 2.082 1.00 26.39 ATOM 1329 N SER A 702 5.851 11.1722.764 1.00 36.40 ATOM 1330 CA SER A 702 6.218 11.787 1.488 1.00 38.48ATOM 1331 CB SER A 702 6.077 13.303 1.581 1.00 34.20 ATOM 1332 OG SER A702 7.065 13.837 2.446 1.00 34.77 ATOM 1333 C SER A 702 7.639 11.4591.036 1.00 38.77 ATOM 1334 O SER A 702 7.915 11.380 −0.162 1.00 39.14ATOM 1335 N GLY A 703 8.537 11.278 1.997 1.00 37.92 ATOM 1336 CA GLY A703 9.920 10.984 1.673 1.00 37.06 ATOM 1337 C GLY A 703 10.242 9.5561.271 1.00 36.77 ATOM 1338 O GLY A 703 11.329 9.293 0.760 1.00 37.21ATOM 1339 N LEU A 704 9.316 8.628 1.493 1.00 28.47 ATOM 1340 CA LEU A704 9.566 7.231 1.138 1.00 27.53 ATOM 1341 CB LEU A 704 8.446 6.3211.655 1.00 29.58 ATOM 1342 CG LEU A 704 8.208 6.233 3.161 1.00 30.45ATOM 1343 CD1 LEU A 704 7.255 5.088 3.465 1.00 29.64 ATOM 1344 CD2 LEU A704 9.510 6.005 3.855 1.00 30.15 ATOM 1345 C LEU A 704 9.682 7.037−0.364 1.00 26.70 ATOM 1346 O LEU A 704 9.092 7.783 −1.142 1.00 27.33ATOM 1347 N SER A 705 10.450 6.028 −0.762 1.00 29.04 ATOM 1348 CA SER A705 10.606 5.704 −2.171 1.00 28.79 ATOM 1349 CB SER A 705 11.734 4.690−2.369 1.00 23.35 ATOM 1350 OG SER A 705 11.393 3.441 −1.802 1.00 24.99ATOM 1351 C SER A 705 9.275 5.062 −2.540 1.00 29.09 ATOM 1352 O SER A705 8.493 4.712 −1.654 1.00 29.81 ATOM 1353 N ILE A 706 9.019 4.894−3.831 1.00 27.02 ATOM 1354 CA ILE A 706 7.764 4.295 −4.268 1.00 26.47ATOM 1355 CB ILE A 706 7.700 4.211 −5.809 1.00 35.41 ATOM 1356 CG2 ILE A706 6.441 3.472 −6.241 1.00 36.09 ATOM 1357 CG1 ILE A 706 7.728 5.622−6.402 1.00 36.23 ATOM 1358 CD1 ILE A 706 7.821 5.658 −7.917 1.00 36.02ATOM 1359 C ILE A 706 7.561 2.902 −3.681 1.00 26.18 ATOM 1360 O ILE A706 6.487 2.584 −3.175 1.00 26.02 ATOM 1361 N GLU A 707 8.594 2.071−3.736 1.00 25.11 ATOM 1362 CA GLU A 707 8.484 0.720 −3.206 1.00 25.30ATOM 1363 CB GLU A 707 9.725 −0.092 −3.577 1.00 46.28 ATOM 1364 CG GLU A707 9.775 −0.446 −5.051 1.00 47.07 ATOM 1365 CD GLU A 707 8.667 −1.406−5.452 1.00 47.32 ATOM 1366 OE1 GLU A 707 8.296 −1.422 −6.645 1.00 47.31ATOM 1367 OE2 GLU A 707 8.177 −2.153 −4.576 1.00 47.02 ATOM 1368 C GLU A707 8.284 0.730 −1.692 1.00 25.18 ATOM 1369 O GLU A 707 7.483 −0.042−1.164 1.00 24.41 ATOM 1370 N GLU A 708 9.005 1.610 −1.002 1.00 23.37ATOM 1371 CA GLU A 708 8.887 1.708 0.448 1.00 24.60 ATOM 1372 CB GLU A708 9.904 2.704 1.011 1.00 30.84 ATOM 1373 CG GLU A 708 11.278 2.1001.265 1.00 31.16 ATOM 1374 CD GLU A 708 12.236 3.077 1.921 1.00 31.10ATOM 1375 OE1 GLU A 708 13.164 2.615 2.617 1.00 31.36 ATOM 1376 OE2 GLUA 708 12.073 4.301 1.732 1.00 31.87 ATOM 1377 C GLU A 708 7.481 2.1380.839 1.00 24.78 ATOM 1378 O GLU A 708 6.886 1.579 1.768 1.00 23.94 ATOM1379 N TYR A 709 6.961 3.133 0.128 1.00 23.21 ATOM 1380 CA TYR A 7095.619 3.644 0.390 1.00 25.29 ATOM 1381 CB TYR A 709 5.295 4.802 −0.5501.00 27.48 ATOM 1382 CG TYR A 709 3.912 5.365 −0.325 1.00 28.20 ATOM1383 CD1 TYR A 709 3.654 6.221 0.743 1.00 28.35 ATOM 1384 CE1 TYR A 7092.375 6.712 0.980 1.00 28.11 ATOM 1385 CD2 TYR A 709 2.853 5.011 −1.1571.00 29.10 ATOM 1386 CE2 TYR A 709 1.567 5.496 −0.927 1.00 29.20 ATOM1387 CZ TYR A 709 1.337 6.343 0.142 1.00 29.09 ATOM 1388 OH TYR A 7090.065 6.813 0.379 1.00 28.65 ATOM 1389 C TYR A 709 4.568 2.549 0.2241.00 25.53 ATOM 1390 O TYR A 709 3.740 2.336 1.111 1.00 24.94 ATOM 1391N LYS A 710 4.602 1.859 −0.915 1.00 25.86 ATOM 1392 CA LYS A 710 3.6580.778 −1.191 1.00 26.20 ATOM 1393 CB LYS A 710 3.955 0.144 −2.551 1.0048.58 ATOM 1394 CG LYS A 710 3.417 −1.276 −2.683 1.00 49.43 ATOM 1395 CDLYS A 710 3.795 −1.914 −4.008 1.00 49.56 ATOM 1396 CE LYS A 710 3.501−3.408 −3.993 1.00 49.72 ATOM 1397 NZ LYS A 710 2.086 −3.707 −3.633 1.0049.51 ATOM 1398 C LYS A 710 3.689 −0.309 −0.123 1.00 25.97 ATOM 1399 OLYS A 710 2.640 −0.743 0.356 1.00 25.66 ATOM 1400 N THR A 711 4.891−0.756 0.236 1.00 24.32 ATOM 1401 CA THR A 711 5.049 −1.800 1.240 1.0023.82 ATOM 1402 CB THR A 711 6.528 −2.205 1.399 1.00 33.44 ATOM 1403 OG1THR A 711 7.030 −2.673 0.141 1.00 33.80 ATOM 1404 CG2 THR A 711 6.669−3.307 2.441 1.00 33.11 ATOM 1405 C THR A 711 4.523 −1.346 2.596 1.0023.74 ATOM 1406 O THR A 711 3.861 −2.106 3.295 1.00 24.01 ATOM 1407 NTHR A 712 4.813 −0.100 2.951 1.00 22.39 ATOM 1408 CA THR A 712 4.3790.449 4.227 1.00 21.87 ATOM 1409 CB THR A 712 5.003 1.831 4.468 1.0023.06 ATOM 1410 OG1 THR A 712 6.432 1.713 4.416 1.00 24.85 ATOM 1411 CG2THR A 712 4.604 2.371 5.832 1.00 23.79 ATOM 1412 C THR A 712 2.859 0.5484.330 1.00 21.27 ATOM 1413 O THR A 712 2.287 0.150 5.340 1.00 22.87 ATOM1414 N LEU A 713 2.207 1.060 3.291 1.00 23.23 ATOM 1415 CA LEU A 7130.751 1.189 3.314 1.00 22.85 ATOM 1416 CB LEU A 713 0.249 1.892 2.0491.00 31.38 ATOM 1417 CG LEU A 713 −0.070 3.382 2.200 1.00 32.26 ATOM1418 CD1 LEU A 713 −1.303 3.560 3.082 1.00 32.03 ATOM 1419 CD2 LEU A 7131.117 4.106 2.804 1.00 32.84 ATOM 1420 C LEU A 713 0.051 −0.154 3.4731.00 22.64 ATOM 1421 O LEU A 713 −0.966 −0.251 4.159 1.00 22.10 ATOM1422 N LYS A 714 0.605 −1.187 2.844 1.00 20.65 ATOM 1423 CA LYS A 7140.054 −2.534 2.919 1.00 20.74 ATOM 1424 CB LYS A 714 0.822 −3.457 1.9701.00 43.81 ATOM 1425 CG LYS A 714 0.599 −4.943 2.199 1.00 44.63 ATOM1426 CD LYS A 714 1.492 −5.772 1.278 1.00 44.93 ATOM 1427 CE LYS A 7141.524 −7.235 1.692 1.00 44.98 ATOM 1428 NZ LYS A 714 0.178 −7.868 1.6471.00 44.80 ATOM 1429 C LYS A 714 0.165 −3.051 4.348 1.00 19.68 ATOM 1430O LYS A 714 −0.755 −3.693 4.865 1.00 20.74 ATOM 1431 N ILE A 715 1.300−2.777 4.984 1.00 20.42 ATOM 1432 CA ILE A 715 1.504 −3.216 6.348 1.0020.28 ATOM 1433 CB ILE A 715 2.950 −2.960 6.818 1.00 24.09 ATOM 1434 CG2ILE A 715 3.105 −3.399 8.264 1.00 24.82 ATOM 1435 CG1 ILE A 715 3.930−3.718 5.917 1.00 25.35 ATOM 1436 CD1 ILE A 715 5.381 −3.440 6.231 1.0024.56 ATOM 1437 C ILE A 715 0.539 −2.476 7.257 1.00 19.19 ATOM 1438 OILE A 715 −0.035 −3.073 8.161 1.00 19.49 ATOM 1439 N ILE A 716 0.367−1.180 7.005 1.00 19.27 ATOM 1440 CA ILE A 716 −0.546 −0.361 7.800 1.0018.10 ATOM 1441 CB ILE A 716 −0.519 1.112 7.345 1.00 20.08 ATOM 1442 CG2ILE A 716 −1.672 1.877 7.984 1.00 20.73 ATOM 1443 CG1 ILE A 716 0.8281.743 7.717 1.00 19.90 ATOM 1444 CD1 ILE A 716 1.027 3.151 7.204 1.0020.14 ATOM 1445 C ILE A 716 −1.977 −0.890 7.705 1.00 16.92 ATOM 1446 OILE A 716 −2.647 −1.066 8.727 1.00 17.86 ATOM 1447 N LYS A 717 −2.449−1.143 6.488 1.00 18.04 ATOM 1448 CA LYS A 717 −3.808 −1.656 6.315 1.0019.57 ATOM 1449 CB LYS A 717 −4.150 −1.839 4.834 1.00 22.85 ATOM 1450 CGLYS A 717 −5.590 −2.297 4.619 1.00 22.42 ATOM 1451 CD LYS A 717 −5.930−2.486 3.144 1.00 23.58 ATOM 1452 CE LYS A 717 −7.357 −2.986 2.980 1.0022.98 ATOM 1453 NZ LYS A 717 −7.730 −3.216 1.552 1.00 24.81 ATOM 1454 CLYS A 717 −3.977 −2.985 7.042 1.00 19.43 ATOM 1455 O LYS A 717 −4.957−3.197 7.753 1.00 18.92 ATOM 1456 N GLN A 718 −3.024 −3.894 6.870 1.0019.29 ATOM 1457 CA GLN A 718 −3.136 −5.173 7.552 1.00 17.73 ATOM 1458 CBGLN A 718 −2.009 −6.099 7.096 1.00 35.14 ATOM 1459 CG GLN A 718 −2.134−6.456 5.621 1.00 35.99 ATOM 1460 CD GLN A 718 −0.956 −7.249 5.095 1.0036.88 ATOM 1461 OE1 GLN A 718 −0.973 −7.718 3.956 1.00 37.13 ATOM 1462NE2 GLN A 718 0.076 −7.396 5.915 1.00 36.21 ATOM 1463 C GLN A 718 −3.144−5.031 9.073 1.00 16.21 ATOM 1464 O GLN A 718 −3.899 −5.725 9.764 1.0016.17 ATOM 1465 N ALA A 719 −2.326 −4.117 9.585 1.00 17.17 ATOM 1466 CAALA A 719 −2.236 −3.886 11.020 1.00 16.40 ATOM 1467 CB ALA A 719 −1.062−2.939 11.335 1.00 18.08 ATOM 1468 C ALA A 719 −3.542 −3.325 11.577 1.0015.71 ATOM 1469 O ALA A 719 −3.996 −3.754 12.637 1.00 15.47 ATOM 1470 NILE A 720 −4.150 −2.380 10.864 1.00 15.28 ATOM 1471 CA ILE A 720 −5.402−1.802 11.330 1.00 17.34 ATOM 1472 CB ILE A 720 −5.758 −0.520 10.5251.00 16.58 ATOM 1473 CG2 ILE A 720 −7.185 −0.054 10.855 1.00 17.16 ATOM1474 CG1 ILE A 720 −4.736 0.570 10.852 1.00 17.26 ATOM 1475 CD1 ILE A720 −5.042 1.931 10.241 1.00 17.39 ATOM 1476 C ILE A 720 −6.516 −2.84711.257 1.00 14.75 ATOM 1477 O ILE A 720 −7.288 −3.002 12.199 1.00 16.06ATOM 1478 N LEU A 721 −6.583 −3.605 10.165 1.00 16.72 ATOM 1479 CA LEU A721 −7.617 −4.629 10.070 1.00 17.03 ATOM 1480 CB LEU A 721 −7.616 −5.2828.684 1.00 21.51 ATOM 1481 CG LEU A 721 −8.136 −4.398 7.544 1.00 22.77ATOM 1482 CD1 LEU A 721 −8.089 −5.164 6.236 1.00 22.53 ATOM 1483 CD2 LEUA 721 −9.556 −3.947 7.834 1.00 22.98 ATOM 1484 C LEU A 721 −7.442 −5.69411.148 1.00 15.19 ATOM 1485 O LEU A 721 −8.416 −6.269 11.624 1.00 16.45ATOM 1486 N ALA A 722 −6.199 −5.940 11.546 1.00 17.48 ATOM 1487 CA ALA A722 −5.924 −6.935 12.571 1.00 17.80 ATOM 1488 CB ALA A 722 −4.431 −7.11312.735 1.00 18.14 ATOM 1489 C ALA A 722 −6.547 −6.557 13.905 1.00 18.00ATOM 1490 O ALA A 722 −6.764 −7.420 14.750 1.00 18.41 ATOM 1491 N THR A723 −6.854 −5.274 14.094 1.00 15.61 ATOM 1492 CA THR A 723 −7.434 −4.85615.359 1.00 15.90 ATOM 1493 CB THR A 723 −7.199 −3.360 15.650 1.00 16.83ATOM 1494 OG1 THR A 723 −7.801 −2.550 14.635 1.00 17.34 ATOM 1495 CG2THR A 723 −5.701 −3.084 15.726 1.00 18.33 ATOM 1496 C THR A 723 −8.909−5.192 15.499 1.00 16.50 ATOM 1497 O THR A 723 −9.542 −4.838 16.492 1.0017.29 ATOM 1498 N ASP A 724 −9.452 −5.875 14.498 1.00 17.56 ATOM 1499 CAASP A 724 −10.826 −6.342 14.549 1.00 18.40 ATOM 1500 CB ASP A 724−11.304 −6.762 13.157 1.00 16.11 ATOM 1501 CG ASP A 724 −12.737 −7.27313.160 1.00 14.99 ATOM 1502 OD1 ASP A 724 −13.297 −7.492 14.254 1.0016.02 ATOM 1503 OD2 ASP A 724 −13.310 −7.458 12.069 1.00 18.73 ATOM 1504C ASP A 724 −10.707 −7.582 15.431 1.00 18.02 ATOM 1505 O ASP A 724−10.114 −8.571 15.006 1.00 18.53 ATOM 1506 N LEU A 725 −11.242 −7.53616.649 1.00 20.52 ATOM 1507 CA LEU A 725 −11.140 −8.685 17.545 1.0021.37 ATOM 1508 CB LEU A 725 −11.851 −8.407 18.873 1.00 31.10 ATOM 1509CG LEU A 725 −10.960 −7.911 20.016 1.00 32.17 ATOM 1510 CD1 LEU A 725−11.782 −7.798 21.293 1.00 32.32 ATOM 1511 CD2 LEU A 725 −9.809 −8.88520.232 1.00 31.61 ATOM 1512 C LEU A 725 −11.673 −9.981 16.942 1.00 22.61ATOM 1513 O LEU A 725 −11.229 −11.061 17.316 1.00 22.86 ATOM 1514 N ALAA 726 −12.613 −9.887 16.006 1.00 24.20 ATOM 1515 CA ALA A 726 −13.158−11.095 15.376 1.00 26.25 ATOM 1516 CB ALA A 726 −14.375 −10.746 14.5201.00 26.36 ATOM 1517 C ALA A 726 −12.093 −11.782 14.520 1.00 25.26 ATOM1518 O ALA A 726 −12.043 −13.015 14.431 1.00 26.23 ATOM 1519 N LEU A 727−11.253 −10.981 13.879 1.00 25.84 ATOM 1520 CA LEU A 727 −10.183 −11.49713.037 1.00 27.01 ATOM 1521 CB LEU A 727 −9.582 −10.354 12.217 1.0027.22 ATOM 1522 CG LEU A 727 −9.355 −10.566 10.718 1.00 29.26 ATOM 1523CD1 LEU A 727 −10.607 −11.167 10.073 1.00 27.54 ATOM 1524 CD2 LEU A 727−9.011 −9.229 10.069 1.00 28.24 ATOM 1525 C LEU A 727 −9.123 −12.11813.946 1.00 26.83 ATOM 1526 O LEU A 727 −8.441 −13.077 13.575 1.00 27.75ATOM 1527 N TYR A 728 −8.982 −11.566 15.144 1.00 23.72 ATOM 1528 CA TYRA 728 −8.013 −12.096 16.094 1.00 24.54 ATOM 1529 CB TYR A 728 −7.843−11.144 17.280 1.00 26.68 ATOM 1530 CG TYR A 728 −7.128 −11.784 18.4401.00 27.14 ATOM 1531 CD1 TYR A 728 −7.828 −12.208 19.568 1.00 27.32 ATOM1532 CE1 TYR A 728 −7.183 −12.878 20.602 1.00 27.41 ATOM 1533 CD2 TYR A728 −5.762 −12.040 18.377 1.00 27.43 ATOM 1534 CE2 TYR A 728 −5.111−12.709 19.400 1.00 27.27 ATOM 1535 CZ TYR A 728 −5.825 −13.126 20.5051.00 27.40 ATOM 1536 OH TYR A 728 −5.178 −13.810 21.507 1.00 28.59 ATOM1537 C TYR A 728 −8.483 −13.462 16.593 1.00 24.46 ATOM 1538 O TYR A 728−7.713 −14.425 16.643 1.00 24.91 ATOM 1539 N ILE A 729 −9.753 −13.53616.968 1.00 25.84 ATOM 1540 CA ILE A 729 −10.335 −14.779 17.463 1.0026.31 ATOM 1541 CB ILE A 729 −11.803 −14.555 17.876 1.00 28.61 ATOM 1542CG2 ILE A 729 −12.482 −15.887 18.155 1.00 28.30 ATOM 1543 CG1 ILE A 729−11.855 −13.646 19.106 1.00 27.91 ATOM 1544 CD1 ILE A 729 −13.251−13.165 19.462 1.00 28.85 ATOM 1545 C ILE A 729 −10.265 −15.874 16.4011.00 28.18 ATOM 1546 O ILE A 729 −10.162 −17.061 16.727 1.00 28.43 ATOM1547 N LYS A 730 −10.304 −15.469 15.135 1.00 32.05 ATOM 1548 CA LYS A730 −10.265 −16.402 14.008 1.00 33.23 ATOM 1549 CB LYS A 730 −10.833−15.714 12.758 1.00 40.71 ATOM 1550 CG LYS A 730 −10.709 −16.526 11.4751.00 40.87 ATOM 1551 CD LYS A 730 −11.146 −15.727 10.251 1.00 40.83 ATOM1552 CE LYS A 730 −11.013 −16.555 8.977 1.00 41.35 ATOM 1553 NZ LYS A730 −11.478 −15.810 7.772 1.00 41.21 ATOM 1554 C LYS A 730 −8.865−16.938 13.697 1.00 33.75 ATOM 1555 O LYS A 730 −8.688 −18.137 13.4571.00 33.39 ATOM 1556 N ARG A 731 −7.876 −16.050 13.703 1.00 31.85 ATOM1557 CA ARG A 731 −6.503 −16.428 13.380 1.00 31.83 ATOM 1558 CB ARG A731 −5.825 −15.293 12.604 1.00 43.64 ATOM 1559 CG ARG A 731 −6.375−15.070 11.205 1.00 44.14 ATOM 1560 CD ARG A 731 −5.975 −13.707 10.6441.00 44.16 ATOM 1561 NE ARG A 731 −4.534 −13.536 10.456 1.00 44.52 ATOM1562 CZ ARG A 731 −3.809 −14.173 9.541 1.00 44.27 ATOM 1563 NH1 ARG A731 −4.383 −15.039 8.716 1.00 44.55 ATOM 1564 NH2 ARG A 731 −2.507−13.933 9.440 1.00 44.01 ATOM 1565 C ARG A 731 −5.603 −16.813 14.5491.00 31.39 ATOM 1566 O ARG A 731 −4.510 −17.339 14.333 1.00 31.88 ATOM1567 N ARG A 732 −6.040 −16.566 15.780 1.00 27.33 ATOM 1568 CA ARG A 732−5.189 −16.880 16.923 1.00 27.09 ATOM 1569 CB ARG A 732 −5.783 −16.31518.218 1.00 27.95 ATOM 1570 CG ARG A 732 −7.063 −16.972 18.680 1.0027.63 ATOM 1571 CD ARG A 732 −7.423 −16.469 20.056 1.00 27.47 ATOM 1572NE ARG A 732 −8.557 −17.178 20.632 1.00 27.81 ATOM 1573 CZ ARG A 732−8.915 −17.083 21.907 1.00 28.15 ATOM 1574 NH1 ARG A 732 −8.225 −16.30822.735 1.00 28.26 ATOM 1575 NH2 ARG A 732 −9.955 −17.772 22.358 1.0029.20 ATOM 1576 C ARG A 732 −4.928 −18.372 17.086 1.00 26.60 ATOM 1577 OARG A 732 −3.853 −18.767 17.524 1.00 26.91 ATOM 1578 N GLY A 733 −5.909−19.195 16.733 1.00 28.21 ATOM 1579 CA GLY A 733 −5.741 −20.633 16.8601.00 28.94 ATOM 1580 C GLY A 733 −4.533 −21.138 16.097 1.00 28.70 ATOM1581 O GLY A 733 −3.785 −21.991 16.582 1.00 29.01 ATOM 1582 N GLU A 734−4.344 −20.609 14.895 1.00 26.13 ATOM 1583 CA GLU A 734 −3.224 −20.99914.049 1.00 26.64 ATOM 1584 CB GLU A 734 −3.257 −20.213 12.741 1.0032.54 ATOM 1585 CG GLU A 734 −2.289 −20.720 11.697 1.00 32.73 ATOM 1586CD GLU A 734 −2.261 −19.855 10.458 1.00 32.93 ATOM 1587 OE1 GLU A 734−3.330 −19.331 10.068 1.00 32.62 ATOM 1588 OE2 GLU A 734 −1.168 −19.7139.867 1.00 33.12 ATOM 1589 C GLU A 734 −1.927 −20.705 14.783 1.00 26.89ATOM 1590 O GLU A 734 −1.071 −21.571 14.935 1.00 26.89 ATOM 1591 N PHE A735 −1.797 −19.463 15.233 1.00 26.37 ATOM 1592 CA PHE A 735 −0.630−18.996 15.965 1.00 26.70 ATOM 1593 CB PHE A 735 −0.911 −17.569 16.4551.00 35.10 ATOM 1594 CG PHE A 735 0.263 −16.884 17.099 1.00 35.60 ATOM1595 CD1 PHE A 735 1.487 −16.801 16.448 1.00 35.44 ATOM 1596 CD2 PHE A735 0.116 −16.256 18.333 1.00 35.57 ATOM 1597 CE1 PHE A 735 2.549−16.098 17.013 1.00 35.65 ATOM 1598 CE2 PHE A 735 1.168 −15.550 18.9091.00 35.48 ATOM 1599 CZ PHE A 735 2.388 −15.469 18.247 1.00 35.90 ATOM1600 C PHE A 735 −0.309 −19.919 17.148 1.00 26.06 ATOM 1601 O PHE A 7350.819 −20.387 17.297 1.00 26.34 ATOM 1602 N PHE A 736 −1.313 −20.18617.978 1.00 27.83 ATOM 1603 CA PHE A 736 −1.144 −21.049 19.146 1.0027.77 ATOM 1604 CB PHE A 736 −2.462 −21.134 19.925 1.00 26.06 ATOM 1605CG PHE A 736 −2.927 −19.810 20.492 1.00 26.21 ATOM 1606 CD1 PHE A 736−4.239 −19.659 20.948 1.00 25.79 ATOM 1607 CD2 PHE A 736 −2.059 −18.72720.587 1.00 25.60 ATOM 1608 CE1 PHE A 736 −4.676 −18.450 21.489 1.0025.76 ATOM 1609 CE2 PHE A 736 −2.490 −17.508 21.130 1.00 25.65 ATOM 1610CZ PHE A 736 −3.801 −17.376 21.580 1.00 25.15 ATOM 1611 C PHE A 736−0.692 −22.453 18.737 1.00 27.64 ATOM 1612 O PHE A 736 0.212 −23.02019.352 1.00 28.68 ATOM 1613 N GLU A 737 −1.335 −23.001 17.709 1.00 26.38ATOM 1614 CA GLU A 737 −1.015 −24.335 17.187 1.00 26.87 ATOM 1615 CB GLUA 737 −1.860 −24.633 15.943 1.00 54.89 ATOM 1616 CG GLU A 737 −3.324−24.925 16.215 1.00 55.77 ATOM 1617 CD GLU A 737 −3.541 −26.319 16.7651.00 56.24 ATOM 1618 OE1 GLU A 737 −3.171 −27.293 16.074 1.00 56.16 ATOM1619 OE2 GLU A 737 −4.081 −26.440 17.885 1.00 55.95 ATOM 1620 C GLU A737 0.458 −24.431 16.809 1.00 26.60 ATOM 1621 O GLU A 737 1.158 −25.38517.181 1.00 24.87 ATOM 1622 N LEU A 738 0.919 −23.446 16.047 1.00 24.73ATOM 1623 CA LEU A 738 2.304 −23.402 15.603 1.00 25.81 ATOM 1624 CB LEUA 738 2.558 −22.131 14.790 1.00 23.18 ATOM 1625 CG LEU A 738 2.098−22.127 13.326 1.00 24.63 ATOM 1626 CD1 LEU A 738 0.728 −22.761 13.1721.00 25.88 ATOM 1627 CD2 LEU A 738 2.093 −20.699 12.816 1.00 24.42 ATOM1628 C LEU A 738 3.271 −23.459 16.771 1.00 25.22 ATOM 1629 O LEU A 7384.259 −24.190 16.730 1.00 26.20 ATOM 1630 N ILE A 739 2.992 −22.67617.809 1.00 22.89 ATOM 1631 CA ILE A 739 3.851 −22.643 18.983 1.00 23.09ATOM 1632 CB ILE A 739 3.406 −21.531 19.961 1.00 29.33 ATOM 1633 CG2 ILEA 739 4.227 −21.594 21.237 1.00 29.45 ATOM 1634 CG1 ILE A 739 3.554−20.161 19.293 1.00 29.28 ATOM 1635 CD1 ILE A 739 4.978 −19.789 18.9681.00 29.71 ATOM 1636 C ILE A 739 3.850 −23.981 19.717 1.00 23.52 ATOM1637 O ILE A 739 4.904 −24.513 20.040 1.00 24.40 ATOM 1638 N ARG A 7402.665 −24.523 19.971 1.00 25.73 ATOM 1639 CA ARG A 740 2.545 −25.79020.683 1.00 27.35 ATOM 1640 CB ARG A 740 1.070 −26.135 20.897 1.00 48.66ATOM 1641 CG ARG A 740 0.840 −27.418 21.679 1.00 49.28 ATOM 1642 CD ARGA 740 −0.625 −27.566 22.043 1.00 49.58 ATOM 1643 NE ARG A 740 −1.484−27.521 20.863 1.00 49.67 ATOM 1644 CZ ARG A 740 −1.504 −28.454 19.9161.00 49.81 ATOM 1645 NH1 ARG A 740 −0.709 −29.514 20.008 1.00 50.00 ATOM1646 NH2 ARG A 740 −2.317 −28.330 18.876 1.00 49.79 ATOM 1647 C ARG A740 3.241 −26.950 19.975 1.00 27.41 ATOM 1648 O ARG A 740 3.784 −27.84520.628 1.00 27.24 ATOM 1649 N LYS A 741 3.230 −26.935 18.646 1.00 27.03ATOM 1650 CA LYS A 741 3.863 −27.999 17.874 1.00 27.38 ATOM 1651 CB LYSA 741 3.055 −28.279 16.605 1.00 33.72 ATOM 1652 CG LYS A 741 1.670−28.843 16.885 1.00 34.15 ATOM 1653 CD LYS A 741 0.952 −29.259 15.6141.00 34.24 ATOM 1654 CE LYS A 741 −0.401 −29.874 15.943 1.00 34.27 ATOM1655 NZ LYS A 741 −1.166 −30.255 14.726 1.00 34.95 ATOM 1656 C LYS A 7415.315 −27.692 17.511 1.00 27.29 ATOM 1657 O LYS A 741 5.937 −28.43016.745 1.00 28.07 ATOM 1658 N ASN A 742 5.854 −26.606 18.061 1.00 25.30ATOM 1659 CA ASN A 742 7.239 −26.224 17.797 1.00 25.09 ATOM 1660 CB ASNA 742 8.189 −27.297 18.332 1.00 29.88 ATOM 1661 CG ASN A 742 8.202−27.351 19.837 1.00 30.15 ATOM 1662 OD1 ASN A 742 8.592 −26.389 20.4911.00 30.86 ATOM 1663 ND2 ASN A 742 7.768 −28.474 20.400 1.00 30.30 ATOM1664 C ASN A 742 7.498 −26.005 16.318 1.00 24.75 ATOM 1665 O ASN A 7428.526 −26.431 15.782 1.00 23.22 ATOM 1666 N GLN A 743 6.564 −25.31915.665 1.00 27.53 ATOM 1667 CA GLN A 743 6.670 −25.035 14.240 1.00 28.70ATOM 1668 CB GLN A 743 5.451 −25.592 13.495 1.00 37.55 ATOM 1669 CG GLNA 743 5.093 −27.027 13.845 1.00 37.58 ATOM 1670 CD GLN A 743 3.960−27.566 12.992 1.00 38.11 ATOM 1671 OE1 GLN A 743 2.923 −26.918 12.8301.00 38.11 ATOM 1672 NE2 GLN A 743 4.147 −28.763 12.447 1.00 37.75 ATOM1673 C GLN A 743 6.755 −23.533 13.979 1.00 28.82 ATOM 1674 O GLN A 7436.881 −23.105 12.832 1.00 28.92 ATOM 1675 N PHE A 744 6.681 −22.72915.035 1.00 28.91 ATOM 1676 CA PHE A 744 6.743 −21.284 14.850 1.00 29.47ATOM 1677 CB PHE A 744 6.432 −20.556 16.157 1.00 40.72 ATOM 1678 CG PHEA 744 6.298 −19.064 15.997 1.00 40.67 ATOM 1679 CD1 PHE A 744 5.279−18.525 15.214 1.00 41.29 ATOM 1680 CD2 PHE A 744 7.191 −18.200 16.6181.00 41.11 ATOM 1681 CE1 PHE A 744 5.153 −17.145 15.053 1.00 41.25 ATOM1682 CE2 PHE A 744 7.074 −16.819 16.464 1.00 41.16 ATOM 1683 CZ PHE A744 6.053 −16.292 15.680 1.00 41.33 ATOM 1684 C PHE A 744 8.097 −20.81914.326 1.00 29.13 ATOM 1685 O PHE A 744 9.146 −21.260 14.792 1.00 30.17ATOM 1686 N ASN A 745 8.055 −19.921 13.349 1.00 28.18 ATOM 1687 CA ASN A745 9.260 −19.363 12.750 1.00 29.83 ATOM 1688 CB ASN A 745 9.795 −20.27211.648 1.00 38.97 ATOM 1689 CG ASN A 745 10.919 −19.622 10.867 1.0039.20 ATOM 1690 OD1 ASN A 745 11.985 −19.348 11.411 1.00 39.54 ATOM 1691ND2 ASN A 745 10.679 −19.357 9.590 1.00 40.15 ATOM 1692 C ASN A 7458.941 −18.005 12.149 1.00 29.56 ATOM 1693 O ASN A 745 8.208 −17.91411.165 1.00 29.59 ATOM 1694 N LEU A 746 9.499 −16.956 12.741 1.00 38.07ATOM 1695 CA LEU A 746 9.268 −15.597 12.270 1.00 39.23 ATOM 1696 CB LEUA 746 9.822 −14.591 13.280 1.00 38.00 ATOM 1697 CG LEU A 746 8.967−14.381 14.528 1.00 37.62 ATOM 1698 CD1 LEU A 746 9.676 −13.427 15.4751.00 38.20 ATOM 1699 CD2 LEU A 746 7.609 −13.821 14.125 1.00 37.68 ATOM1700 C LEU A 746 9.852 −15.302 10.895 1.00 39.66 ATOM 1701 O LEU A 7469.455 −14.335 10.245 1.00 39.51 ATOM 1702 N GLU A 747 10.792 −16.12810.449 1.00 39.64 ATOM 1703 CA GLU A 747 11.404 −15.918 9.143 1.00 39.71ATOM 1704 CB GLU A 747 12.605 −16.845 8.965 1.00 45.59 ATOM 1705 CG GLUA 747 13.921 −16.094 8.881 1.00 46.56 ATOM 1706 CD GLU A 747 15.125−16.981 9.132 1.00 46.55 ATOM 1707 OE1 GLU A 747 15.305 −17.974 8.3951.00 46.54 ATOM 1708 OE2 GLU A 747 15.890 −16.679 10.072 1.00 46.60 ATOM1709 C GLU A 747 10.391 −16.136 8.029 1.00 38.87 ATOM 1710 O GLU A 74710.422 −15.454 7.002 1.00 39.21 ATOM 1711 N ASP A 748 9.487 −17.0868.234 1.00 32.77 ATOM 1712 CA ASP A 748 8.455 −17.363 7.248 1.00 32.31ATOM 1713 CB ASP A 748 7.654 −18.600 7.652 1.00 47.03 ATOM 1714 CG ASP A748 6.639 −19.002 6.603 1.00 47.67 ATOM 1715 OD1 ASP A 748 5.613 −18.3056.459 1.00 47.81 ATOM 1716 OD2 ASP A 748 6.876 −20.018 5.912 1.00 48.36ATOM 1717 C ASP A 748 7.544 −16.141 7.190 1.00 32.61 ATOM 1718 O ASP A748 6.915 −15.777 8.185 1.00 30.88 ATOM 1719 N PRO A 749 7.466 −15.4906.018 1.00 39.12 ATOM 1720 CD PRO A 749 8.049 −15.930 4.739 1.00 38.16ATOM 1721 CA PRO A 749 6.634 −14.299 5.824 1.00 39.58 ATOM 1722 CB PRO A749 6.773 −14.021 4.325 1.00 38.14 ATOM 1723 CG PRO A 749 7.069 −15.3673.745 1.00 38.10 ATOM 1724 C PRO A 749 5.176 −14.417 6.274 1.00 39.62ATOM 1725 O PRO A 749 4.601 −13.447 6.770 1.00 39.95 ATOM 1726 N HIS A750 4.571 −15.588 6.108 1.00 32.50 ATOM 1727 CA HIS A 750 3.181 −15.7426.524 1.00 31.88 ATOM 1728 CB HIS A 750 2.562 −17.016 5.946 1.00 30.66ATOM 1729 CG HIS A 750 1.149 −17.240 6.384 1.00 30.76 ATOM 1730 CD2 HISA 750 −0.008 −16.667 5.981 1.00 30.83 ATOM 1731 ND1 HIS A 750 0.815−18.097 7.410 1.00 31.54 ATOM 1732 CE1 HIS A 750 −0.488 −18.041 7.6211.00 31.23 ATOM 1733 NE2 HIS A 750 −1.011 −17.180 6.768 1.00 31.56 ATOM1734 C HIS A 750 3.055 −15.761 8.042 1.00 31.66 ATOM 1735 O HIS A 7502.146 −15.148 8.604 1.00 31.17 ATOM 1736 N GLU A 751 3.957 −16.470 8.7111.00 31.26 ATOM 1737 CA GLU A 751 3.913 −16.519 10.165 1.00 31.20 ATOM1738 CB GLU A 751 4.898 −17.563 10.703 1.00 33.16 ATOM 1739 CG GLU A 7514.444 −19.000 10.455 1.00 33.17 ATOM 1740 CD GLU A 751 5.215 −20.01711.274 1.00 33.56 ATOM 1741 OE1 GLU A 751 5.432 −19.772 12.478 1.0033.10 ATOM 1742 OE2 GLU A 751 5.587 −21.071 10.720 1.00 33.79 ATOM 1743C GLU A 751 4.247 −15.127 10.699 1.00 31.23 ATOM 1744 O GLU A 751 3.836−14.753 11.800 1.00 31.00 ATOM 1745 N LYS A 752 4.979 −14.364 9.892 1.0029.23 ATOM 1746 CA LYS A 752 5.372 −13.008 10.239 1.00 29.88 ATOM 1747CB LYS A 752 6.292 −12.439 9.154 1.00 37.79 ATOM 1748 CG LYS A 752 6.867−11.058 9.453 1.00 38.37 ATOM 1749 CD LYS A 752 7.766 −11.087 10.6841.00 38.41 ATOM 1750 CE LYS A 752 8.526 −9.783 10.861 1.00 38.61 ATOM1751 NZ LYS A 752 9.473 −9.521 9.748 1.00 38.19 ATOM 1752 C LYS A 7524.143 −12.120 10.373 1.00 29.16 ATOM 1753 O LYS A 752 3.921 −11.51011.425 1.00 29.42 ATOM 1754 N GLU A 753 3.341 −12.029 9.315 1.00 30.11ATOM 1755 CA GLU A 753 2.156 −11.191 9.402 1.00 30.60 ATOM 1756 CB GLU A753 1.467 −11.040 8.038 1.00 54.85 ATOM 1757 CG GLU A 753 1.100 −12.3167.315 1.00 55.61 ATOM 1758 CD GLU A 753 0.501 −12.034 5.942 1.00 55.82ATOM 1759 OE1 GLU A 753 1.195 −11.420 5.102 1.00 55.58 ATOM 1760 OE2 GLUA 753 −0.663 −12.420 5.705 1.00 55.80 ATOM 1761 C GLU A 753 1.201−11.736 10.458 1.00 29.96 ATOM 1762 O GLU A 753 0.476 −10.973 11.0941.00 30.36 ATOM 1763 N LEU A 754 1.215 −13.050 10.668 1.00 25.09 ATOM1764 CA LEU A 754 0.364 −13.638 11.695 1.00 23.83 ATOM 1765 CB LEU A 7540.510 −15.160 11.719 1.00 25.34 ATOM 1766 CG LEU A 754 −0.242 −15.85712.852 1.00 26.46 ATOM 1767 CD1 LEU A 754 −1.730 −15.558 12.759 1.0025.32 ATOM 1768 CD2 LEU A 754 0.010 −17.364 12.767 1.00 25.75 ATOM 1769C LEU A 754 0.812 −13.064 13.039 1.00 23.90 ATOM 1770 O LEU A 754 −0.011−12.728 13.896 1.00 24.10 ATOM 1771 N PHE A 755 2.126 −12.953 13.2151.00 22.27 ATOM 1772 CA PHE A 755 2.673 −12.405 14.444 1.00 23.27 ATOM1773 CB PHE A 755 4.188 −12.601 14.506 1.00 27.67 ATOM 1774 CG PHE A 7554.811 −11.977 15.715 1.00 27.49 ATOM 1775 CD1 PHE A 755 4.559 −12.49216.981 1.00 27.28 ATOM 1776 CD2 PHE A 755 5.589 −10.834 15.596 1.0026.66 ATOM 1777 CE1 PHE A 755 5.070 −11.872 18.117 1.00 28.85 ATOM 1778CE2 PHE A 755 6.108 −10.200 16.727 1.00 27.67 ATOM 1779 CZ PHE A 7555.849 −10.718 17.987 1.00 27.51 ATOM 1780 C PHE A 755 2.352 −10.91414.590 1.00 23.26 ATOM 1781 O PHE A 755 1.932 −10.469 15.665 1.00 22.65ATOM 1782 N LEU A 756 2.553 −10.148 13.520 1.00 21.99 ATOM 1783 CA LEU A756 2.274 −8.712 13.552 1.00 23.22 ATOM 1784 CB LEU A 756 2.593 −8.05912.206 1.00 24.32 ATOM 1785 CG LEU A 756 4.060 −7.993 11.785 1.00 25.68ATOM 1786 CD1 LEU A 756 4.163 −7.476 10.364 1.00 24.86 ATOM 1787 CD2 LEUA 756 4.821 −7.094 12.737 1.00 25.84 ATOM 1788 C LEU A 756 0.820 −8.43513.906 1.00 22.88 ATOM 1789 O LEU A 756 0.520 −7.441 14.561 1.00 22.05ATOM 1790 N ALA A 757 −0.078 −9.316 13.477 1.00 22.97 ATOM 1791 CA ALA A757 −1.498 −9.152 13.770 1.00 22.24 ATOM 1792 CB ALA A 757 −2.326−10.143 12.950 1.00 21.11 ATOM 1793 C ALA A 757 −1.733 −9.387 15.2551.00 23.73 ATOM 1794 O ALA A 757 −2.491 −8.668 15.907 1.00 22.64 ATOM1795 N MET A 758 −1.080 −10.407 15.794 1.00 17.51 ATOM 1796 CA MET A 758−1.234 −10.717 17.198 1.00 18.28 ATOM 1797 CB MET A 758 −0.581 −12.07217.503 1.00 27.85 ATOM 1798 CG MET A 758 −1.181 −13.255 16.720 1.0027.03 ATOM 1799 SD MET A 758 −2.826 −13.794 17.241 1.00 29.72 ATOM 1800CE MET A 758 −3.778 −13.473 15.747 1.00 28.03 ATOM 1801 C MET A 758−0.608 −9.605 18.039 1.00 17.15 ATOM 1802 O MET A 758 −1.088 −9.31919.137 1.00 18.07 ATOM 1803 N LEU A 759 0.447 −8.979 17.515 1.00 17.47ATOM 1804 CA LEU A 759 1.139 −7.898 18.225 1.00 19.04 ATOM 1805 CB LEU A759 2.418 −7.482 17.491 1.00 19.37 ATOM 1806 CG LEU A 759 3.214 −6.32818.112 1.00 20.18 ATOM 1807 CD1 LEU A 759 3.610 −6.669 19.550 1.00 21.45ATOM 1808 CD2 LEU A 759 4.439 −6.039 17.261 1.00 21.48 ATOM 1809 C LEU A759 0.213 −6.699 18.342 1.00 19.95 ATOM 1810 O LEU A 759 0.119 −6.08119.406 1.00 18.11 ATOM 1811 N MET A 760 −0.454 −6.367 17.240 1.00 17.24ATOM 1812 CA MET A 760 −1.393 −5.240 17.251 1.00 17.90 ATOM 1813 CB META 760 −2.032 −5.063 15.874 1.00 18.91 ATOM 1814 CG MET A 760 −1.140−4.422 14.835 1.00 19.09 ATOM 1815 SD MET A 760 −0.717 −2.696 15.2161.00 18.56 ATOM 1816 CE MET A 760 −2.370 −1.939 15.227 1.00 17.91 ATOM1817 C MET A 760 −2.468 −5.487 18.302 1.00 18.32 ATOM 1818 O MET A 760−2.808 −4.590 19.072 1.00 15.93 ATOM 1819 N THR A 761 −3.002 −6.70618.350 1.00 17.94 ATOM 1820 CA THR A 761 −4.024 −7.021 19.336 1.00 17.15ATOM 1821 CB THR A 761 −4.540 −8.454 19.164 1.00 18.32 ATOM 1822 OG1 THRA 761 −5.103 −8.594 17.856 1.00 18.56 ATOM 1823 CG2 THR A 761 −5.594−8.772 20.220 1.00 17.55 ATOM 1824 C THR A 761 −3.446 −6.880 20.746 1.0017.99 ATOM 1825 O THR A 761 −4.089 −6.332 21.635 1.00 19.05 ATOM 1826 NALA A 762 −2.228 −7.381 20.946 1.00 16.64 ATOM 1827 CA ALA A 762 −1.590−7.298 22.255 1.00 16.82 ATOM 1828 CB ALA A 762 −0.194 −7.908 22.2021.00 19.67 ATOM 1829 C ALA A 762 −1.514 −5.854 22.755 1.00 18.11 ATOM1830 O ALA A 762 −1.766 −5.585 23.933 1.00 16.84 ATOM 1831 N CYS A 763−1.169 −4.936 21.860 1.00 15.07 ATOM 1832 CA CYS A 763 −1.081 −3.52322.216 1.00 16.86 ATOM 1833 CB CYS A 763 −0.303 −2.767 21.147 1.00 16.42ATOM 1834 SG CYS A 763 1.450 −3.220 21.036 1.00 16.68 ATOM 1835 C CYS A763 −2.469 −2.904 22.372 1.00 18.36 ATOM 1836 O CYS A 763 −2.705 −2.09123.269 1.00 15.92 ATOM 1837 N ASP A 764 −3.385 −3.289 21.494 1.00 17.47ATOM 1838 CA ASP A 764 −4.743 −2.766 21.528 1.00 18.98 ATOM 1839 CB ASPA 764 −5.539 −3.360 20.360 1.00 18.28 ATOM 1840 CG ASP A 764 −6.834−2.624 20.089 1.00 19.27 ATOM 1841 OD1 ASP A 764 −7.670 −3.161 19.3331.00 22.03 ATOM 1842 OD2 ASP A 764 −7.013 −1.507 20.614 1.00 18.63 ATOM1843 C ASP A 764 −5.446 −3.078 22.857 1.00 18.67 ATOM 1844 O ASP A 764−6.269 −2.290 23.331 1.00 19.51 ATOM 1845 N LEU A 765 −5.126 −4.21723.470 1.00 16.07 ATOM 1846 CA LEU A 765 −5.771 −4.596 24.726 1.00 16.91ATOM 1847 CB LEU A 765 −6.108 −6.098 24.712 1.00 22.31 ATOM 1848 CG LEUA 765 −6.925 −6.653 23.540 1.00 22.32 ATOM 1849 CD1 LEU A 765 −7.143−8.152 23.733 1.00 22.41 ATOM 1850 CD2 LEU A 765 −8.260 −5.940 23.4511.00 22.60 ATOM 1851 C LEU A 765 −4.911 −4.288 25.953 1.00 17.63 ATOM1852 O LEU A 765 −5.250 −4.699 27.062 1.00 18.64 ATOM 1853 N SER A 766−3.830 −3.541 25.750 1.00 17.02 ATOM 1854 CA SER A 766 −2.869 −3.23026.812 1.00 18.24 ATOM 1855 CB SER A 766 −1.846 −2.205 26.312 1.00 20.09ATOM 1856 OG SER A 766 −2.378 −0.892 26.319 1.00 21.90 ATOM 1857 C SER A766 −3.400 −2.775 28.171 1.00 17.35 ATOM 1858 O SER A 766 −2.738 −2.97529.197 1.00 16.73 ATOM 1859 N ALA A 767 −4.571 −2.152 28.196 1.00 18.41ATOM 1860 CA ALA A 767 −5.113 −1.682 29.466 1.00 19.58 ATOM 1861 CB ALAA 767 −6.465 −0.994 29.242 1.00 14.05 ATOM 1862 C ALA A 767 −5.272−2.823 30.461 1.00 20.35 ATOM 1863 O ALA A 767 −5.111 −2.636 31.666 1.0020.93 ATOM 1864 N ILE A 768 −5.580 −4.008 29.949 1.00 18.87 ATOM 1865 CAILE A 768 −5.789 −5.176 30.786 1.00 20.62 ATOM 1866 CB ILE A 768 −6.405−6.330 29.943 1.00 19.42 ATOM 1867 CG2 ILE A 768 −5.323 −7.008 29.1121.00 20.41 ATOM 1868 CG1 ILE A 768 −7.087 −7.351 30.856 1.00 20.44 ATOM1869 CD1 ILE A 768 −8.333 −6.831 31.548 1.00 20.90 ATOM 1870 C ILE A 768−4.499 −5.657 31.466 1.00 20.39 ATOM 1871 O ILE A 768 −4.543 −6.54432.307 1.00 21.21 ATOM 1872 N THR A 769 −3.364 −5.061 31.108 1.00 19.18ATOM 1873 CA THR A 769 −2.075 −5.437 31.693 1.00 19.16 ATOM 1874 CB THRA 769 −0.996 −5.672 30.620 1.00 20.58 ATOM 1875 OG1 THR A 769 −0.519−4.408 30.131 1.00 19.24 ATOM 1876 CG2 THR A 769 −1.561 −6.478 29.4531.00 20.09 ATOM 1877 C THR A 769 −1.496 −4.379 32.637 1.00 21.13 ATOM1878 O THR A 769 −0.488 −4.618 33.300 1.00 21.47 ATOM 1879 N LYS A 770−2.127 −3.214 32.691 1.00 19.99 ATOM 1880 CA LYS A 770 −1.634 −2.12033.527 1.00 20.68 ATOM 1881 CB LYS A 770 −2.313 −0.812 33.108 1.00 20.27ATOM 1882 CG LYS A 770 −2.103 −0.409 31.660 1.00 19.98 ATOM 1883 CD LYSA 770 −0.711 0.136 31.431 1.00 20.21 ATOM 1884 CE LYS A 770 −0.502 0.46429.960 1.00 20.34 ATOM 1885 NZ LYS A 770 0.829 1.065 29.701 1.00 21.28ATOM 1886 C LYS A 770 −1.861 −2.330 35.026 1.00 19.97 ATOM 1887 O LYS A770 −2.628 −3.204 35.437 1.00 20.86 ATOM 1888 N PRO A 771 −1.186 −1.52135.866 1.00 23.24 ATOM 1889 CD PRO A 771 −0.150 −0.537 35.512 1.00 25.67ATOM 1890 CA PRO A 771 −1.329 −1.615 37.321 1.00 24.06 ATOM 1891 CB PROA 771 −0.461 −0.463 37.823 1.00 25.01 ATOM 1892 CG PRO A 771 0.636−0.421 36.809 1.00 24.38 ATOM 1893 C PRO A 771 −2.804 −1.429 37.672 1.0023.94 ATOM 1894 O PRO A 771 −3.529 −0.723 36.970 1.00 23.81 ATOM 1895 NTRP A 772 −3.236 −2.057 38.759 1.00 22.70 ATOM 1896 CA TRP A 772 −4.626−2.009 39.201 1.00 23.47 ATOM 1897 CB TRP A 772 −4.721 −2.480 40.6521.00 31.03 ATOM 1898 CG TRP A 772 −6.120 −2.631 41.148 1.00 31.98 ATOM1899 CD2 TRP A 772 −7.205 −3.295 40.484 1.00 31.41 ATOM 1900 CE2 TRP A772 −8.322 −3.228 41.345 1.00 32.26 ATOM 1901 CE3 TRP A 772 −7.342−3.940 39.246 1.00 31.94 ATOM 1902 CD1 TRP A 772 −6.611 −2.199 42.3461.00 31.60 ATOM 1903 NE1 TRP A 772 −7.930 −2.553 42.471 1.00 31.93 ATOM1904 CZ2 TRP A 772 −9.565 −3.785 41.009 1.00 32.15 ATOM 1905 CZ3 TRP A772 −8.579 −4.493 38.912 1.00 31.45 ATOM 1906 CH2 TRP A 772 −9.672−4.411 39.792 1.00 31.98 ATOM 1907 C TRP A 772 −5.368 −0.678 39.057 1.0023.85 ATOM 1908 O TRP A 772 −6.409 −0.609 38.399 1.00 22.22 ATOM 1909 NPRO A 773 −4.857 0.398 39.678 1.00 25.77 ATOM 1910 CD PRO A 773 −3.5830.541 40.403 1.00 32.22 ATOM 1911 CA PRO A 773 −5.546 1.689 39.567 1.0026.04 ATOM 1912 CB PRO A 773 −4.609 2.650 40.304 1.00 32.61 ATOM 1913 CGPRO A 773 −3.259 1.991 40.171 1.00 33.14 ATOM 1914 C PRO A 773 −5.8312.122 38.134 1.00 25.71 ATOM 1915 O PRO A 773 −6.900 2.653 37.834 1.0026.03 ATOM 1916 N ILE A 774 −4.869 1.885 37.253 1.00 21.46 ATOM 1917 CAILE A 774 −5.008 2.236 35.850 1.00 20.45 ATOM 1918 CB ILE A 774 −3.6482.105 35.135 1.00 25.41 ATOM 1919 CG2 ILE A 774 −3.790 2.436 33.654 1.0025.27 ATOM 1920 CG1 ILE A 774 −2.633 3.037 35.802 1.00 26.17 ATOM 1921CD1 ILE A 774 −1.205 2.807 35.355 1.00 25.47 ATOM 1922 C ILE A 774−6.038 1.329 35.173 1.00 19.51 ATOM 1923 O ILE A 774 −6.928 1.804 34.4711.00 18.75 ATOM 1924 N GLN A 775 −5.925 0.021 35.388 1.00 22.02 ATOM1925 CA GLN A 775 −6.868 −0.916 34.783 1.00 21.75 ATOM 1926 CB GLN A 775−6.491 −2.361 35.135 1.00 20.94 ATOM 1927 CG GLN A 775 −7.668 −3.34035.192 1.00 21.03 ATOM 1928 CD GLN A 775 −8.395 −3.531 33.864 1.00 21.36ATOM 1929 OE1 GLN A 775 −9.457 −4.141 33.826 1.00 21.09 ATOM 1930 NE2GLN A 775 −7.826 −3.018 32.779 1.00 21.40 ATOM 1931 C GLN A 775 −8.300−0.626 35.219 1.00 21.97 ATOM 1932 O GLN A 775 −9.216 −0.637 34.402 1.0021.91 ATOM 1933 N GLN A 776 −8.486 −0.372 36.510 1.00 21.52 ATOM 1934 CAGLN A 776 −9.807 −0.066 37.051 1.00 23.77 ATOM 1935 CB GLN A 776 −9.7090.263 38.537 1.00 38.83 ATOM 1936 CG GLN A 776 −9.798 −0.919 39.456 1.0039.61 ATOM 1937 CD GLN A 776 −9.747 −0.503 40.910 1.00 39.43 ATOM 1938OE1 GLN A 776 −8.717 −0.035 41.397 1.00 39.77 ATOM 1939 NE2 GLN A 776−10.865 −0.662 41.610 1.00 39.38 ATOM 1940 C GLN A 776 −10.420 1.13336.350 1.00 23.07 ATOM 1941 O GLN A 776 −11.582 1.106 35.942 1.00 24.26ATOM 1942 N ARG A 777 −9.628 2.190 36.231 1.00 23.71 ATOM 1943 CA ARG A777 −10.081 3.413 35.598 1.00 23.28 ATOM 1944 CB ARG A 777 −8.993 4.48935.692 1.00 27.59 ATOM 1945 CG ARG A 777 −9.423 5.850 35.159 1.00 27.74ATOM 1946 CD ARG A 777 −8.305 6.873 35.280 1.00 27.86 ATOM 1947 NE ARG A777 −7.155 6.535 34.445 1.00 27.75 ATOM 1948 CZ ARG A 777 −7.161 6.54533.114 1.00 27.57 ATOM 1949 NH1 ARG A 777 −8.257 6.881 32.448 1.00 28.23ATOM 1950 NH2 ARG A 777 −6.066 6.216 32.446 1.00 28.20 ATOM 1951 C ARG A777 −10.465 3.191 34.139 1.00 23.20 ATOM 1952 O ARG A 777 −11.537 3.60533.704 1.00 22.51 ATOM 1953 N ILE A 778 −9.592 2.535 33.380 1.00 17.78ATOM 1954 CA ILE A 778 −9.884 2.297 31.972 1.00 17.96 ATOM 1955 CB ILE A778 −8.633 1.806 31.225 1.00 19.43 ATOM 1956 CG2 ILE A 778 −8.967 1.52029.764 1.00 18.09 ATOM 1957 CG1 ILE A 778 −7.560 2.894 31.305 1.00 19.35ATOM 1958 CD1 ILE A 778 −6.214 2.505 30.738 1.00 19.60 ATOM 1959 C ILE A778 −11.038 1.323 31.796 1.00 18.56 ATOM 1960 O ILE A 778 −11.872 1.50230.903 1.00 18.79 ATOM 1961 N ALA A 779 −11.106 0.309 32.654 1.00 20.16ATOM 1962 CA ALA A 779 −12.199 −0.656 32.590 1.00 21.21 ATOM 1963 CB ALAA 779 −12.066 −1.680 33.708 1.00 24.43 ATOM 1964 C ALA A 779 −13.5310.091 32.712 1.00 21.19 ATOM 1965 O ALA A 779 −14.519 −0.280 32.085 1.0020.38 ATOM 1966 N GLU A 780 −13.558 1.147 33.518 1.00 20.96 ATOM 1967 CAGLU A 780 −14.786 1.926 33.682 1.00 22.15 ATOM 1968 CB GLU A 780 −14.6522.894 34.863 1.00 51.37 ATOM 1969 CG GLU A 780 −14.497 2.196 36.206 1.0052.40 ATOM 1970 CD GLU A 780 −14.449 3.163 37.373 1.00 53.03 ATOM 1971OE1 GLU A 780 −13.590 4.072 37.359 1.00 53.05 ATOM 1972 OE2 GLU A 780−15.266 3.013 38.306 1.00 52.97 ATOM 1973 C GLU A 780 −15.147 2.69632.407 1.00 21.53 ATOM 1974 O GLU A 780 −16.326 2.918 32.127 1.00 20.90ATOM 1975 N LEU A 781 −14.134 3.105 31.642 1.00 18.46 ATOM 1976 CA LEU A781 −14.365 3.818 30.390 1.00 19.53 ATOM 1977 CB LEU A 781 −13.050 4.39929.847 1.00 20.51 ATOM 1978 CG LEU A 781 −12.392 5.516 30.672 1.00 21.84ATOM 1979 CD1 LEU A 781 −11.131 6.026 29.976 1.00 21.36 ATOM 1980 CD2LEU A 781 −13.389 6.660 30.828 1.00 20.48 ATOM 1981 C LEU A 781 −14.9492.824 29.389 1.00 19.65 ATOM 1982 O LEU A 781 −15.898 3.133 28.654 1.0019.62 ATOM 1983 N VAL A 782 −14.368 1.628 29.362 1.00 21.76 ATOM 1984 CAVAL A 782 −14.837 0.569 28.474 1.00 22.54 ATOM 1985 CB VAL A 782 −14.026−0.740 28.693 1.00 22.92 ATOM 1986 CG1 VAL A 782 −14.659 −1.889 27.9311.00 21.63 ATOM 1987 CG2 VAL A 782 −12.588 −0.554 28.231 1.00 22.05 ATOM1988 C VAL A 782 −16.311 0.290 28.766 1.00 21.93 ATOM 1989 O VAL A 782−17.142 0.238 27.857 1.00 23.01 ATOM 1990 N ALA A 783 −16.632 0.12330.045 1.00 19.50 ATOM 1991 CA ALA A 783 −18.000 −0.166 30.445 1.0021.17 ATOM 1992 CB ALA A 783 −18.061 −0.447 31.942 1.00 21.14 ATOM 1993C ALA A 783 −18.940 0.979 30.078 1.00 20.67 ATOM 1994 O ALA A 783−20.051 0.755 29.598 1.00 21.82 ATOM 1995 N THR A 784 −18.490 2.20930.291 1.00 23.13 ATOM 1996 CA THR A 784 −19.312 3.362 29.962 1.00 23.26ATOM 1997 CB THR A 784 −18.577 4.668 30.312 1.00 24.94 ATOM 1998 OG1 THRA 784 −18.379 4.726 31.731 1.00 25.01 ATOM 1999 CG2 THR A 784 −19.3795.877 29.864 1.00 24.89 ATOM 2000 C THR A 784 −19.702 3.364 28.481 1.0024.33 ATOM 2001 O THR A 784 −20.881 3.543 28.130 1.00 22.64 ATOM 2002 NGLU A 785 −18.720 3.153 27.612 1.00 19.82 ATOM 2003 CA GLU A 785 −18.9913.136 26.182 1.00 21.00 ATOM 2004 CB GLU A 785 −17.678 2.998 25.387 1.0021.06 ATOM 2005 CG GLU A 785 −17.871 2.918 23.873 1.00 20.31 ATOM 2006CD GLU A 785 −16.575 3.080 23.081 1.00 21.05 ATOM 2007 OE1 GLU A 785−16.506 2.557 21.947 1.00 20.57 ATOM 2008 OE2 GLU A 785 −15.637 3.74023.572 1.00 18.86 ATOM 2009 C GLU A 785 −19.965 2.006 25.846 1.00 20.29ATOM 2010 O GLU A 785 −20.905 2.211 25.083 1.00 20.32 ATOM 2011 N PHE A786 −19.753 0.824 26.422 1.00 21.26 ATOM 2012 CA PHE A 786 −20.643−0.307 26.161 1.00 21.97 ATOM 2013 CB PHE A 786 −20.185 −1.567 26.9011.00 26.06 ATOM 2014 CG PHE A 786 −18.955 −2.216 26.324 1.00 27.41 ATOM2015 CD1 PHE A 786 −18.629 −2.067 24.978 1.00 27.06 ATOM 2016 CD2 PHE A786 −18.146 −3.021 27.122 1.00 26.60 ATOM 2017 CE1 PHE A 786 −17.519−2.711 24.437 1.00 27.27 ATOM 2018 CE2 PHE A 786 −17.032 −3.672 26.5861.00 27.24 ATOM 2019 CZ PHE A 786 −16.722 −3.515 25.244 1.00 27.18 ATOM2020 C PHE A 786 −22.068 0.011 26.599 1.00 23.40 ATOM 2021 O PHE A 786−23.023 −0.269 25.878 1.00 21.69 ATOM 2022 N PHE A 787 −22.206 0.59427.787 1.00 23.44 ATOM 2023 CA PHE A 787 −23.530 0.926 28.297 1.00 22.70ATOM 2024 CB PHE A 787 −23.445 1.413 29.751 1.00 22.93 ATOM 2025 CG PHEA 787 −22.945 0.370 30.719 1.00 21.91 ATOM 2026 CD1 PHE A 787 −23.122−0.991 30.464 1.00 22.94 ATOM 2027 CD2 PHE A 787 −22.335 0.749 31.9101.00 23.07 ATOM 2028 CE1 PHE A 787 −22.697 −1.954 31.383 1.00 23.17 ATOM2029 CE2 PHE A 787 −21.907 −0.201 32.833 1.00 22.50 ATOM 2030 CZ PHE A787 −22.087 −1.555 32.572 1.00 23.33 ATOM 2031 C PHE A 787 −24.215 1.96827.417 1.00 23.79 ATOM 2032 O PHE A 787 −25.431 1.906 27.205 1.00 21.92ATOM 2033 N ASP A 788 −23.442 2.912 26.884 1.00 23.70 ATOM 2034 CA ASP A788 −24.021 3.923 26.010 1.00 25.33 ATOM 2035 CB ASP A 788 −22.978 4.95925.591 1.00 54.55 ATOM 2036 CG ASP A 788 −23.605 6.296 25.233 1.00 55.82ATOM 2037 OD1 ASP A 788 −24.157 6.955 26.141 1.00 56.10 ATOM 2038 OD2ASP A 788 −23.558 6.686 24.046 1.00 55.97 ATOM 2039 C ASP A 788 −24.5713.216 24.774 1.00 24.36 ATOM 2040 O ASP A 788 −25.646 3.551 24.283 1.0025.06 ATOM 2041 N GLN A 789 −23.837 2.235 24.257 1.00 20.19 ATOM 2042 CAGLN A 789 −24.350 1.522 23.101 1.00 19.43 ATOM 2043 CB GLN A 789 −23.3400.508 22.566 1.00 19.05 ATOM 2044 CG GLN A 789 −23.987 −0.433 21.5631.00 19.55 ATOM 2045 CD GLN A 789 −23.011 −1.268 20.781 1.00 19.48 ATOM2046 OE1 GLN A 789 −23.388 −2.299 20.222 1.00 20.82 ATOM 2047 NE2 GLN A789 −21.755 −0.833 20.718 1.00 18.14 ATOM 2048 C GLN A 789 −25.629 0.80223.503 1.00 20.46 ATOM 2049 O GLN A 789 −26.586 0.735 22.729 1.00 20.11ATOM 2050 N GLY A 790 −25.639 0.266 24.721 1.00 22.31 ATOM 2051 CA GLY A790 −26.810 −0.436 25.216 1.00 24.09 ATOM 2052 C GLY A 790 −28.031 0.46325.175 1.00 25.10 ATOM 2053 O GLY A 790 −29.115 0.025 24.783 1.00 24.31ATOM 2054 N ASP A 791 −27.857 1.722 25.573 1.00 25.00 ATOM 2055 CA ASP A791 −28.963 2.683 25.568 1.00 25.93 ATOM 2056 CB ASP A 791 −28.525 4.02626.160 1.00 29.26 ATOM 2057 CG ASP A 791 −28.107 3.918 27.611 1.00 29.25ATOM 2058 OD1 ASP A 791 −28.575 2.987 28.297 1.00 29.11 ATOM 2059 OD2ASP A 791 −27.323 4.778 28.068 1.00 30.04 ATOM 2060 C ASP A 791 −29.4642.909 24.143 1.00 25.33 ATOM 2061 O ASP A 791 −30.669 3.029 23.907 1.0026.34 ATOM 2062 N ARG A 792 −28.527 2.984 23.205 1.00 25.90 ATOM 2063 CAARG A 792 −28.842 3.185 21.794 1.00 25.99 ATOM 2064 CB ARG A 792 −27.5463.326 20.990 1.00 34.02 ATOM 2065 CG ARG A 792 −26.801 4.633 21.228 1.0034.62 ATOM 2066 CD ARG A 792 −27.310 5.716 20.300 1.00 35.57 ATOM 2067NE ARG A 792 −26.820 5.533 18.935 1.00 35.28 ATOM 2068 CZ ARG A 792−25.591 5.845 18.537 1.00 34.46 ATOM 2069 NH1 ARG A 792 −24.726 6.35819.403 1.00 34.52 ATOM 2070 NH2 ARG A 792 −25.225 5.647 17.278 1.0034.52 ATOM 2071 C ARG A 792 −29.645 2.005 21.261 1.00 26.14 ATOM 2072 OARG A 792 −30.634 2.179 20.553 1.00 26.08 ATOM 2073 N GLU A 793 −29.2190.797 21.608 1.00 25.23 ATOM 2074 CA GLU A 793 −29.910 −0.396 21.1411.00 25.15 ATOM 2075 CB GLU A 793 −29.156 −1.650 21.584 1.00 28.67 ATOM2076 CG GLU A 793 −27.715 −1.688 21.120 1.00 29.21 ATOM 2077 CD GLU A793 −27.005 −2.958 21.543 1.00 29.03 ATOM 2078 OE1 GLU A 793 −27.219−3.406 22.689 1.00 28.67 ATOM 2079 OE2 GLU A 793 −26.222 −3.501 20.7371.00 28.60 ATOM 2080 C GLU A 793 −31.343 −0.444 21.660 1.00 26.11 ATOM2081 O GLU A 793 −32.254 −0.858 20.945 1.00 25.51 ATOM 2082 N ARG A 794−31.546 −0.022 22.904 1.00 30.47 ATOM 2083 CA ARG A 794 −32.887 −0.04123.477 1.00 30.88 ATOM 2084 CB ARG A 794 −32.861 0.402 24.945 1.00 42.43ATOM 2085 CG ARG A 794 −31.776 −0.241 25.786 1.00 42.99 ATOM 2086 CD ARGA 794 −31.978 0.056 27.266 1.00 43.11 ATOM 2087 NE ARG A 794 −32.839−0.939 27.893 1.00 43.32 ATOM 2088 CZ ARG A 794 −32.425 −1.820 28.7981.00 42.83 ATOM 2089 NH1 ARG A 794 −31.158 −1.826 29.194 1.00 43.06 ATOM2090 NH2 ARG A 794 −33.274 −2.708 29.295 1.00 43.25 ATOM 2091 C ARG A794 −33.818 0.886 22.701 1.00 31.12 ATOM 2092 O ARG A 794 −34.972 0.54722.451 1.00 30.32 ATOM 2093 N LYS A 795 −33.307 2.050 22.314 1.00 28.47ATOM 2094 CA LYS A 795 −34.111 3.036 21.597 1.00 30.19 ATOM 2095 CB LYSA 795 −33.538 4.438 21.833 1.00 43.10 ATOM 2096 CG LYS A 795 −33.0844.688 23.262 1.00 43.51 ATOM 2097 CD LYS A 795 −32.642 6.129 23.482 1.0044.03 ATOM 2098 CE LYS A 795 −33.794 6.991 23.976 1.00 43.69 ATOM 2099NZ LYS A 795 −34.961 6.964 23.051 1.00 43.61 ATOM 2100 C LYS A 795−34.238 2.799 20.093 1.00 29.44 ATOM 2101 O LYS A 795 −35.341 2.83219.545 1.00 29.39 ATOM 2102 N GLU A 796 −33.110 2.558 19.433 1.00 32.97ATOM 2103 CA GLU A 796 −33.080 2.358 17.987 1.00 33.23 ATOM 2104 CB GLUA 796 −31.723 2.803 17.443 1.00 31.41 ATOM 2105 CG GLU A 796 −31.2654.158 17.957 1.00 31.18 ATOM 2106 CD GLU A 796 −29.913 4.573 17.401 1.0031.42 ATOM 2107 OE1 GLU A 796 −29.334 5.558 17.904 1.00 31.78 ATOM 2108OE2 GLU A 796 −29.432 3.917 16.455 1.00 32.26 ATOM 2109 C GLU A 796−33.376 0.939 17.496 1.00 33.01 ATOM 2110 O GLU A 796 −33.778 0.75016.347 1.00 33.78 ATOM 2111 N LEU A 797 −33.170 −0.058 18.347 1.00 29.85ATOM 2112 CA LEU A 797 −33.424 −1.438 17.952 1.00 29.25 ATOM 2113 CB LEUA 797 −32.134 −2.261 18.059 1.00 32.07 ATOM 2114 CG LEU A 797 −30.951−1.828 17.185 1.00 32.45 ATOM 2115 CD1 LEU A 797 −29.759 −2.731 17.4751.00 32.42 ATOM 2116 CD2 LEU A 797 −31.325 −1.904 15.709 1.00 32.29 ATOM2117 C LEU A 797 −34.513 −2.073 18.807 1.00 29.52 ATOM 2118 O LEU A 797−34.954 −3.192 18.534 1.00 29.88 ATOM 2119 N ASN A 798 −34.940 −1.34819.839 1.00 31.24 ATOM 2120 CA ASN A 798 −35.972 −1.815 20.757 1.0031.79 ATOM 2121 CB ASN A 798 −37.332 −1.805 20.062 1.00 46.67 ATOM 2122CG ASN A 798 −37.975 −0.439 20.083 1.00 47.32 ATOM 2123 OD1 ASN A 798−38.405 0.038 21.136 1.00 47.67 ATOM 2124 ND2 ASN A 798 −38.037 0.20818.924 1.00 47.41 ATOM 2125 C ASN A 798 −35.694 −3.189 21.338 1.00 31.17ATOM 2126 O ASN A 798 −36.593 −4.016 21.468 1.00 30.69 ATOM 2127 N ILE A799 −34.438 −3.427 21.694 1.00 29.19 ATOM 2128 CA ILE A 799 −34.046−4.701 22.274 1.00 29.70 ATOM 2129 CB ILE A 799 −33.026 −5.444 21.3791.00 28.41 ATOM 2130 CG2 ILE A 799 −33.660 −5.795 20.036 1.00 29.14 ATOM2131 CG1 ILE A 799 −31.781 −4.571 21.191 1.00 28.71 ATOM 2132 CD1 ILE A799 −30.632 −5.251 20.494 1.00 28.52 ATOM 2133 C ILE A 799 −33.389−4.463 23.627 1.00 29.70 ATOM 2134 O ILE A 799 −32.889 −3.370 23.9041.00 29.11 ATOM 2135 N GLU A 800 −33.410 −5.481 24.477 1.00 31.12 ATOM2136 CA GLU A 800 −32.764 −5.369 25.775 1.00 32.32 ATOM 2137 CB GLU A800 −33.322 −6.394 26.768 1.00 47.83 ATOM 2138 CG GLU A 800 −32.572−6.418 28.099 1.00 48.49 ATOM 2139 CD GLU A 800 −32.999 −7.559 29.0071.00 48.67 ATOM 2140 OE1 GLU A 800 −32.393 −7.713 30.091 1.00 48.86 ATOM2141 OE2 GLU A 800 −33.938 −8.299 28.640 1.00 48.41 ATOM 2142 C GLU A800 −31.309 −5.692 25.474 1.00 31.85 ATOM 2143 O GLU A 800 −31.009−6.731 24.888 1.00 31.72 ATOM 2144 N PRO A 801 −30.386 −4.801 25.8551.00 32.29 ATOM 2145 CD PRO A 801 −30.534 −3.557 26.629 1.00 32.84 ATOM2146 CA PRO A 801 −28.976 −5.083 25.578 1.00 32.39 ATOM 2147 CB PRO A801 −28.281 −3.798 26.019 1.00 33.48 ATOM 2148 CG PRO A 801 −29.143−3.351 27.168 1.00 33.84 ATOM 2149 C PRO A 801 −28.462 −6.308 26.3231.00 31.89 ATOM 2150 O PRO A 801 −29.056 −6.752 27.312 1.00 31.79 ATOM2151 N THR A 802 −27.362 −6.863 25.826 1.00 28.76 ATOM 2152 CA THR A 802−26.739 −8.016 26.456 1.00 28.15 ATOM 2153 CB THR A 802 −25.626 −8.60325.569 1.00 44.26 ATOM 2154 OG1 THR A 802 −25.026 −9.721 26.233 1.0045.50 ATOM 2155 CG2 THR A 802 −24.561 −7.555 25.282 1.00 44.69 ATOM 2156C THR A 802 −26.139 −7.521 27.767 1.00 28.29 ATOM 2157 O THR A 802−25.956 −6.317 27.960 1.00 27.03 ATOM 2158 N ASP A 803 −25.843 −8.44828.669 1.00 28.44 ATOM 2159 CA ASP A 803 −25.275 −8.094 29.963 1.0028.64 ATOM 2160 CB ASP A 803 −24.779 −9.358 30.667 1.00 34.48 ATOM 2161CG ASP A 803 −25.893 −10.098 31.379 1.00 34.81 ATOM 2162 OD1 ASP A 803−27.045 −10.054 30.893 1.00 34.90 ATOM 2163 OD2 ASP A 803 −25.611−10.730 32.420 1.00 35.01 ATOM 2164 C ASP A 803 −24.153 −7.063 29.9061.00 28.44 ATOM 2165 O ASP A 803 −24.176 −6.074 30.635 1.00 28.48 ATOM2166 N LEU A 804 −23.177 −7.275 29.031 1.00 25.97 ATOM 2167 CA LEU A 804−22.058 −6.348 28.952 1.00 26.25 ATOM 2168 CB LEU A 804 −20.951 −6.93728.075 1.00 47.64 ATOM 2169 CG LEU A 804 −21.304 −7.412 26.671 1.0048.05 ATOM 2170 CD1 LEU A 804 −21.264 −6.244 25.708 1.00 48.53 ATOM 2171CD2 LEU A 804 −20.301 −8.466 26.242 1.00 48.25 ATOM 2172 C LEU A 804−22.415 −4.938 28.501 1.00 26.00 ATOM 2173 O LEU A 804 −21.654 −4.00728.728 1.00 25.68 ATOM 2174 N MET A 805 −23.576 −4.763 27.881 1.00 25.47ATOM 2175 CA MET A 805 −23.971 −3.427 27.445 1.00 25.62 ATOM 2176 CB META 805 −24.246 −3.422 25.940 1.00 32.20 ATOM 2177 CG MET A 805 −22.992−3.634 25.113 1.00 31.73 ATOM 2178 SD MET A 805 −23.263 −3.668 23.3451.00 32.78 ATOM 2179 CE MET A 805 −21.557 −3.485 22.751 1.00 31.70 ATOM2180 C MET A 805 −25.186 −2.920 28.209 1.00 24.74 ATOM 2181 O MET A 805−25.808 −1.932 27.813 1.00 25.55 ATOM 2182 N ASN A 806 −25.502 −3.59629.311 1.00 23.96 ATOM 2183 CA ASN A 806 −26.645 −3.239 30.151 1.0025.57 ATOM 2184 CB ASN A 806 −27.467 −4.495 30.463 1.00 28.17 ATOM 2185CG ASN A 806 −28.738 −4.190 31.241 1.00 28.82 ATOM 2186 OD1 ASN A 806−28.985 −3.049 31.628 1.00 28.36 ATOM 2187 ND2 ASN A 806 −29.550 −5.21631.474 1.00 28.76 ATOM 2188 C ASN A 806 −26.159 −2.592 31.448 1.00 25.52ATOM 2189 O ASN A 806 −25.648 −3.273 32.338 1.00 25.16 ATOM 2190 N ARG A807 −26.321 −1.276 31.544 1.00 25.21 ATOM 2191 CA ARG A 807 −25.892−0.512 32.717 1.00 25.42 ATOM 2192 CB ARG A 807 −26.254 0.963 32.5321.00 30.28 ATOM 2193 CG ARG A 807 −25.516 1.919 33.450 1.00 31.10 ATOM2194 CD ARG A 807 −26.051 3.331 33.290 1.00 31.22 ATOM 2195 NE ARG A 807−26.092 3.752 31.892 1.00 31.51 ATOM 2196 CZ ARG A 807 −25.040 4.15731.192 1.00 31.00 ATOM 2197 NH1 ARG A 807 −23.839 4.205 31.753 1.0032.13 ATOM 2198 NH2 ARG A 807 −25.191 4.516 29.923 1.00 30.26 ATOM 2199C ARG A 807 −26.528 −1.030 34.002 1.00 27.00 ATOM 2200 O ARG A 807−25.916 −0.988 35.073 1.00 26.42 ATOM 2201 N GLU A 808 −27.762 −1.50833.895 1.00 29.47 ATOM 2202 CA GLU A 808 −28.477 −2.031 35.053 1.0030.52 ATOM 2203 CB GLU A 808 −29.914 −2.372 34.659 1.00 44.58 ATOM 2204CG GLU A 808 −30.775 −1.147 34.408 1.00 45.18 ATOM 2205 CD GLU A 808−32.132 −1.492 33.837 1.00 45.51 ATOM 2206 OE1 GLU A 808 −32.761 −2.45134.332 1.00 45.53 ATOM 2207 OE2 GLU A 808 −32.573 −0.796 32.898 1.0045.65 ATOM 2208 C GLU A 808 −27.780 −3.261 35.629 1.00 30.44 ATOM 2209 OGLU A 808 −27.875 −3.542 36.828 1.00 30.33 ATOM 2210 N LYS A 809 −27.077−3.985 34.765 1.00 31.29 ATOM 2211 CA LYS A 809 −26.355 −5.190 35.1621.00 31.25 ATOM 2212 CB LYS A 809 −26.522 −6.279 34.092 1.00 41.16 ATOM2213 CG LYS A 809 −27.951 −6.773 33.888 1.00 41.47 ATOM 2214 CD LYS A809 −28.391 −7.716 34.995 1.00 41.55 ATOM 2215 CE LYS A 809 −27.714−9.075 34.885 1.00 41.48 ATOM 2216 NZ LYS A 809 −28.230 −9.865 33.7331.00 41.41 ATOM 2217 C LYS A 809 −24.870 −4.879 35.338 1.00 30.98 ATOM2218 O LYS A 809 −24.023 −5.744 35.129 1.00 30.77 ATOM 2219 N LYS A 810−24.551 −3.646 35.721 1.00 26.58 ATOM 2220 CA LYS A 810 −23.155 −3.25935.901 1.00 26.99 ATOM 2221 CB LYS A 810 −23.050 −1.768 36.235 1.0043.46 ATOM 2222 CG LYS A 810 −23.626 −1.387 37.587 1.00 44.21 ATOM 2223CD LYS A 810 −23.413 0.090 37.878 1.00 44.21 ATOM 2224 CE LYS A 810−23.942 0.459 39.256 1.00 44.19 ATOM 2225 NZ LYS A 810 −23.718 1.89739.566 1.00 44.47 ATOM 2226 C LYS A 810 −22.462 −4.077 36.997 1.00 26.09ATOM 2227 O LYS A 810 −21.234 −4.128 37.060 1.00 26.59 ATOM 2228 N ASN A811 −23.250 −4.720 37.852 1.00 29.32 ATOM 2229 CA ASN A 811 −22.693−5.526 38.934 1.00 29.87 ATOM 2230 CB ASN A 811 −23.812 −6.017 39.8581.00 45.97 ATOM 2231 CG ASN A 811 −24.632 −7.135 39.240 1.00 46.38 ATOM2232 OD1 ASN A 811 −24.137 −8.247 39.042 1.00 46.84 ATOM 2233 ND2 ASN A811 −25.887 −6.847 38.927 1.00 46.45 ATOM 2234 C ASN A 811 −21.931−6.730 38.385 1.00 29.68 ATOM 2235 O ASN A 811 −21.228 −7.425 39.1211.00 29.10 ATOM 2236 N LYS A 812 −22.075 −6.970 37.086 1.00 24.91 ATOM2237 CA LYS A 812 −21.418 −8.100 36.438 1.00 25.57 ATOM 2238 CB LYS A812 −22.292 −8.623 35.295 1.00 45.40 ATOM 2239 CG LYS A 812 −22.850−10.016 35.509 1.00 46.25 ATOM 2240 CD LYS A 812 −23.811 −10.060 36.6781.00 46.19 ATOM 2241 CE LYS A 812 −24.429 −11.439 36.816 1.00 46.23 ATOM2242 NZ LYS A 812 −23.387 −12.487 37.001 1.00 46.38 ATOM 2243 C LYS A812 −20.025 −7.789 35.886 1.00 24.76 ATOM 2244 O LYS A 812 −19.340−8.688 35.401 1.00 24.68 ATOM 2245 N ILE A 813 −19.598 −6.534 35.9631.00 26.65 ATOM 2246 CA ILE A 813 −18.294 −6.162 35.424 1.00 26.72 ATOM2247 CB ILE A 813 −18.008 −4.656 35.630 1.00 25.86 ATOM 2248 CG2 ILE A813 −16.564 −4.337 35.260 1.00 25.72 ATOM 2249 CG1 ILE A 813 −18.955−3.830 34.751 1.00 25.85 ATOM 2250 CD1 ILE A 813 −18.880 −2.335 34.9841.00 26.75 ATOM 2251 C ILE A 813 −17.123 −6.986 35.957 1.00 26.25 ATOM2252 O ILE A 813 −16.271 −7.426 35.185 1.00 25.98 ATOM 2253 N PRO A 814−17.055 −7.205 37.280 1.00 22.10 ATOM 2254 CD PRO A 814 −17.742 −6.55938.415 1.00 23.22 ATOM 2255 CA PRO A 814 −15.916 −8.003 37.741 1.0023.12 ATOM 2256 CB PRO A 814 −16.116 −8.048 39.253 1.00 22.48 ATOM 2257CG PRO A 814 −16.722 −6.697 39.537 1.00 22.19 ATOM 2258 C PRO A 814−15.842 −9.392 37.115 1.00 23.05 ATOM 2259 O PRO A 814 −14.792 −9.79636.619 1.00 23.01 ATOM 2260 N SER A 815 −16.952 −10.123 37.129 1.0024.56 ATOM 2261 CA SER A 815 −16.955 −11.465 36.555 1.00 24.61 ATOM 2262CB SER A 815 −18.286 −12.174 36.844 1.00 32.62 ATOM 2263 OG SER A 815−19.393 −11.454 36.330 1.00 33.36 ATOM 2264 C SER A 815 −16.687 −11.44035.049 1.00 24.80 ATOM 2265 O SER A 815 −16.055 −12.349 34.513 1.0025.10 ATOM 2266 N MET A 816 −17.153 −10.398 34.368 1.00 25.71 ATOM 2267CA MET A 816 −16.938 −10.286 32.925 1.00 24.80 ATOM 2268 CB MET A 816−17.820 −9.188 32.332 1.00 40.93 ATOM 2269 CG MET A 816 −19.302 −9.43232.489 1.00 41.93 ATOM 2270 SD MET A 816 −20.264 −8.316 31.459 1.0042.83 ATOM 2271 CE MET A 816 −19.866 −6.716 32.201 1.00 41.73 ATOM 2272C MET A 816 −15.479 −10.000 32.585 1.00 24.22 ATOM 2273 O MET A 816−14.969 −10.476 31.574 1.00 24.07 ATOM 2274 N GLN A 817 −14.806 −9.21633.420 1.00 24.08 ATOM 2275 CA GLN A 817 −13.403 −8.909 33.182 1.0022.68 ATOM 2276 CB GLN A 817 −12.904 −7.844 34.161 1.00 21.90 ATOM 2277CG GLN A 817 −13.287 −6.415 33.786 1.00 21.57 ATOM 2278 CD GLN A 817−12.797 −6.020 32.407 1.00 22.28 ATOM 2279 OE1 GLN A 817 −13.389 −6.39231.396 1.00 21.33 ATOM 2280 NE2 GLN A 817 −11.704 −5.272 32.359 1.0021.19 ATOM 2281 C GLN A 817 −12.587 −10.185 33.344 1.00 24.08 ATOM 2282O GLN A 817 −11.655 −10.435 32.588 1.00 22.00 ATOM 2283 N VAL A 818−12.947 −10.990 34.340 1.00 22.79 ATOM 2284 CA VAL A 818 −12.262 −12.25634.582 1.00 23.81 ATOM 2285 CB VAL A 818 −12.839 −12.958 35.828 1.0026.49 ATOM 2286 CG1 VAL A 818 −12.225 −14.338 35.983 1.00 26.65 ATOM2287 CG2 VAL A 818 −12.567 −12.115 37.064 1.00 26.49 ATOM 2288 C VAL A818 −12.453 −13.161 33.364 1.00 24.69 ATOM 2289 O VAL A 818 −11.502−13.776 32.871 1.00 23.39 ATOM 2290 N GLY A 819 −13.687 −13.234 32.8781.00 25.13 ATOM 2291 CA GLY A 819 −13.971 −14.061 31.716 1.00 24.79 ATOM2292 C GLY A 819 −13.221 −13.571 30.490 1.00 24.86 ATOM 2293 O GLY A 819−12.729 −14.354 29.677 1.00 25.43 ATOM 2294 N PHE A 820 −13.140 −12.25530.355 1.00 24.15 ATOM 2295 CA PHE A 820 −12.440 −11.635 29.241 1.0022.60 ATOM 2296 CB PHE A 820 −12.606 −10.113 29.336 1.00 22.65 ATOM 2297CG PHE A 820 −11.736 −9.335 28.389 1.00 22.10 ATOM 2298 CD1 PHE A 820−11.863 −9.490 27.011 1.00 22.63 ATOM 2299 CD2 PHE A 820 −10.803 −8.42428.879 1.00 22.66 ATOM 2300 CE1 PHE A 820 −11.069 −8.743 26.133 1.0022.28 ATOM 2301 CE2 PHE A 820 −10.008 −7.677 28.011 1.00 22.73 ATOM 2302CZ PHE A 820 −10.143 −7.839 26.637 1.00 22.74 ATOM 2303 C PHE A 820−10.964 −12.024 29.293 1.00 23.46 ATOM 2304 O PHE A 820 −10.357 −12.36928.283 1.00 21.24 ATOM 2305 N ILE A 821 −10.390 −11.984 30.488 1.0021.23 ATOM 2306 CA ILE A 821 −8.990 −12.323 30.646 1.00 21.89 ATOM 2307CB ILE A 821 −8.525 −12.044 32.088 1.00 22.37 ATOM 2308 CG2 ILE A 821−7.130 −12.596 32.315 1.00 22.42 ATOM 2309 CG1 ILE A 821 −8.526 −10.53432.332 1.00 21.45 ATOM 2310 CD1 ILE A 821 −8.377 −10.160 33.777 1.0023.29 ATOM 2311 C ILE A 821 −8.744 −13.784 30.292 1.00 22.08 ATOM 2312 OILE A 821 −7.864 −14.081 29.488 1.00 24.60 ATOM 2313 N ASP A 822 −9.528−14.687 30.873 1.00 31.25 ATOM 2314 CA ASP A 822 −9.364 −16.113 30.6001.00 32.20 ATOM 2315 CB ASP A 822 −10.379 −16.950 31.390 1.00 31.68 ATOM2316 CG ASP A 822 −10.096 −16.978 32.876 1.00 30.88 ATOM 2317 OD1 ASP A822 −8.923 −16.812 33.265 1.00 31.47 ATOM 2318 OD2 ASP A 822 −11.054−17.186 33.652 1.00 31.29 ATOM 2319 C ASP A 822 −9.520 −16.474 29.1271.00 33.01 ATOM 2320 O ASP A 822 −8.680 −17.165 28.552 1.00 33.17 ATOM2321 N ALA A 823 −10.600 −15.996 28.523 1.00 31.01 ATOM 2322 CA ALA A823 −10.912 −16.309 27.131 1.00 30.74 ATOM 2323 CB ALA A 823 −12.402−16.092 26.894 1.00 28.33 ATOM 2324 C ALA A 823 −10.123 −15.608 26.0301.00 30.37 ATOM 2325 O ALA A 823 −9.919 −16.179 24.959 1.00 30.71 ATOM2326 N ILE A 824 −9.671 −14.385 26.281 1.00 26.40 ATOM 2327 CA ILE A 824−8.968 −13.624 25.250 1.00 25.53 ATOM 2328 CB ILE A 824 −9.761 −12.32524.898 1.00 28.97 ATOM 2329 CG2 ILE A 824 −8.978 −11.487 23.899 1.0029.02 ATOM 2330 CG1 ILE A 824 −11.154 −12.665 24.357 1.00 29.19 ATOM2331 CD1 ILE A 824 −11.151 −13.353 23.013 1.00 29.99 ATOM 2332 C ILE A824 −7.537 −13.185 25.546 1.00 27.07 ATOM 2333 O ILE A 824 −6.639−13.358 24.722 1.00 26.42 ATOM 2334 N CYS A 825 −7.324 −12.617 26.7261.00 24.64 ATOM 2335 CA CYS A 825 −6.020 −12.070 27.075 1.00 24.29 ATOM2336 CB CYS A 825 −6.207 −11.003 28.145 1.00 22.55 ATOM 2337 SG CYS A825 −7.489 −9.813 27.703 1.00 21.61 ATOM 2338 C CYS A 825 −4.878 −12.97927.493 1.00 23.81 ATOM 2339 O CYS A 825 −3.776 −12.856 26.971 1.00 23.60ATOM 2340 N LEU A 826 −5.131 −13.866 28.448 1.00 25.10 ATOM 2341 CA LEUA 826 −4.098 −14.761 28.955 1.00 26.70 ATOM 2342 CB LEU A 826 −4.727−15.770 29.921 1.00 38.73 ATOM 2343 CG LEU A 826 −4.228 −15.764 31.3701.00 39.48 ATOM 2344 CD1 LEU A 826 −4.024 −14.343 31.867 1.00 38.99 ATOM2345 CD2 LEU A 826 −5.230 −16.498 32.243 1.00 39.26 ATOM 2346 C LEU A826 −3.301 −15.492 27.873 1.00 25.78 ATOM 2347 O LEU A 826 −2.072−15.427 27.854 1.00 26.14 ATOM 2348 N GLN A 827 −3.993 −16.179 26.9721.00 26.44 ATOM 2349 CA GLN A 827 −3.308 −16.919 25.920 1.00 26.16 ATOM2350 CB GLN A 827 −4.313 −17.689 25.065 1.00 31.94 ATOM 2351 CG GLN A827 −5.146 −18.687 25.839 1.00 32.38 ATOM 2352 CD GLN A 827 −6.176−19.374 24.967 1.00 33.15 ATOM 2353 OE1 GLN A 827 −5.844 −20.233 24.1461.00 33.30 ATOM 2354 NE2 GLN A 827 −7.437 −18.989 25.130 1.00 33.01 ATOM2355 C GLN A 827 −2.483 −16.005 25.034 1.00 26.24 ATOM 2356 O GLN A 827−1.394 −16.372 24.593 1.00 26.27 ATOM 2357 N LEU A 828 −2.995 −14.81124.761 1.00 23.62 ATOM 2358 CA LEU A 828 −2.256 −13.887 23.912 1.0023.54 ATOM 2359 CB LEU A 828 −3.121 −12.678 23.547 1.00 27.47 ATOM 2360CG LEU A 828 −2.393 −11.621 22.705 1.00 27.18 ATOM 2361 CD1 LEU A 828−1.769 −12.267 21.474 1.00 28.21 ATOM 2362 CD2 LEU A 828 −3.361 −10.53422.293 1.00 27.24 ATOM 2363 C LEU A 828 −0.948 −13.398 24.525 1.00 24.07ATOM 2364 O LEU A 828 0.089 −13.389 23.863 1.00 23.90 ATOM 2365 N TYR A829 −0.984 −12.979 25.785 1.00 22.58 ATOM 2366 CA TYR A 829 0.232−12.492 26.410 1.00 23.51 ATOM 2367 CB TYR A 829 −0.108 −11.655 27.6521.00 22.13 ATOM 2368 CG TYR A 829 −0.797 −10.352 27.273 1.00 22.65 ATOM2369 CD1 TYR A 829 −0.133 −9.395 26.504 1.00 21.70 ATOM 2370 CE1 TYR A829 −0.778 −8.224 26.084 1.00 22.06 ATOM 2371 CD2 TYR A 829 −2.126−10.110 27.622 1.00 22.96 ATOM 2372 CE2 TYR A 829 −2.782 −8.939 27.2021.00 21.69 ATOM 2373 CZ TYR A 829 −2.096 −8.009 26.437 1.00 22.78 ATOM2374 OH TYR A 829 −2.717 −6.850 26.023 1.00 20.96 ATOM 2375 C TYR A 8291.171 −13.653 26.725 1.00 22.44 ATOM 2376 O TYR A 829 2.378 −13.46926.803 1.00 23.40 ATOM 2377 N GLU A 830 0.615 −14.851 26.877 1.00 26.33ATOM 2378 CA GLU A 830 1.451 −16.025 27.127 1.00 27.63 ATOM 2379 CB GLUA 830 0.602 −17.227 27.539 1.00 34.99 ATOM 2380 CG GLU A 830 0.034−17.110 28.941 1.00 35.86 ATOM 2381 CD GLU A 830 −0.865 −18.266 29.3181.00 36.17 ATOM 2382 OE1 GLU A 830 −1.246 −18.349 30.507 1.00 35.89 ATOM2383 OE2 GLU A 830 −1.195 −19.084 28.430 1.00 36.49 ATOM 2384 C GLU A830 2.186 −16.326 25.826 1.00 26.91 ATOM 2385 O GLU A 830 3.383 −16.61425.827 1.00 27.95 ATOM 2386 N ALA A 831 1.465 −16.235 24.711 1.00 26.22ATOM 2387 CA ALA A 831 2.056 −16.489 23.398 1.00 26.36 ATOM 2388 CB ALAA 831 0.965 −16.533 22.328 1.00 20.71 ATOM 2389 C ALA A 831 3.091−15.425 23.044 1.00 25.92 ATOM 2390 O ALA A 831 4.108 −15.725 22.4291.00 26.14 ATOM 2391 N LEU A 832 2.833 −14.180 23.432 1.00 25.86 ATOM2392 CA LEU A 832 3.767 −13.096 23.138 1.00 24.48 ATOM 2393 CB LEU A 8323.127 −11.738 23.447 1.00 23.29 ATOM 2394 CG LEU A 832 4.036 −10.51323.333 1.00 22.75 ATOM 2395 CD1 LEU A 832 4.597 −10.387 21.926 1.0022.85 ATOM 2396 CD2 LEU A 832 3.237 −9.268 23.701 1.00 23.24 ATOM 2397 CLEU A 832 5.056 −13.238 23.936 1.00 25.65 ATOM 2398 O LEU A 832 6.140−12.902 23.454 1.00 25.17 ATOM 2399 N THR A 833 4.931 −13.720 25.1661.00 26.35 ATOM 2400 CA THR A 833 6.092 −13.910 26.021 1.00 27.50 ATOM2401 CB THR A 833 5.654 −14.289 27.446 1.00 28.58 ATOM 2402 OG1 THR A833 4.872 −13.218 27.994 1.00 28.28 ATOM 2403 CG2 THR A 833 6.868−14.531 28.339 1.00 28.51 ATOM 2404 C THR A 833 6.968 −15.007 25.4181.00 28.22 ATOM 2405 O THR A 833 8.197 −14.977 25.540 1.00 28.01 ATOM2406 N HIS A 834 6.333 −15.964 24.750 1.00 32.53 ATOM 2407 CA HIS A 8347.080 −17.044 24.117 1.00 33.13 ATOM 2408 CB HIS A 834 6.131 −18.05323.473 1.00 41.03 ATOM 2409 CG HIS A 834 6.833 −19.200 22.820 1.00 41.66ATOM 2410 CD2 HIS A 834 7.017 −19.505 21.514 1.00 41.45 ATOM 2411 ND1HIS A 834 7.497 −20.170 23.538 1.00 41.66 ATOM 2412 CE1 HIS A 834 8.060−21.024 22.702 1.00 41.76 ATOM 2413 NE2 HIS A 834 7.785 −20.643 21.4671.00 41.58 ATOM 2414 C HIS A 834 7.979 −16.433 23.050 1.00 33.02 ATOM2415 O HIS A 834 9.179 −16.701 23.003 1.00 33.90 ATOM 2416 N VAL A 8357.390 −15.603 22.195 1.00 34.00 ATOM 2417 CA VAL A 835 8.142 −14.94321.136 1.00 33.47 ATOM 2418 CB VAL A 835 7.235 −14.027 20.282 1.00 34.13ATOM 2419 CG1 VAL A 835 8.082 −13.226 19.304 1.00 33.51 ATOM 2420 CG2VAL A 835 6.213 −14.863 19.533 1.00 33.76 ATOM 2421 C VAL A 835 9.278−14.105 21.705 1.00 34.04 ATOM 2422 O VAL A 835 10.373 −14.076 21.1471.00 33.58 ATOM 2423 N SER A 836 9.017 −13.416 22.813 1.00 31.52 ATOM2424 CA SER A 836 10.041 −12.585 23.436 1.00 32.24 ATOM 2425 CB SER A836 10.016 −11.176 22.838 1.00 33.50 ATOM 2426 OG SER A 836 11.125−10.416 23.284 1.00 33.58 ATOM 2427 C SER A 836 9.861 −12.503 24.9491.00 31.70 ATOM 2428 O SER A 836 8.937 −11.856 25.447 1.00 30.73 ATOM2429 N GLU A 837 10.758 −13.168 25.668 1.00 32.13 ATOM 2430 CA GLU A 83710.742 −13.209 27.126 1.00 32.75 ATOM 2431 CB GLU A 837 12.035 −13.86227.624 1.00 50.88 ATOM 2432 CG GLU A 837 13.295 −13.194 27.082 1.0051.44 ATOM 2433 CD GLU A 837 14.564 −13.981 27.368 1.00 51.73 ATOM 2434OE1 GLU A 837 14.863 −14.226 28.558 1.00 51.76 ATOM 2435 OE2 GLU A 83715.264 −14.349 26.399 1.00 51.58 ATOM 2436 C GLU A 837 10.579 −11.83627.779 1.00 32.06 ATOM 2437 O GLU A 837 9.916 −11.702 28.808 1.00 32.57ATOM 2438 N ASP A 838 11.185 −10.821 27.175 1.00 27.93 ATOM 2439 CA ASPA 838 11.135 −9.463 27.699 1.00 28.49 ATOM 2440 CB ASP A 838 12.085−8.574 26.896 1.00 35.78 ATOM 2441 CG ASP A 838 13.511 −9.093 26.9081.00 37.30 ATOM 2442 OD1 ASP A 838 14.167 −9.014 27.969 1.00 36.40 ATOM2443 OD2 ASP A 838 13.971 −9.589 25.857 1.00 37.49 ATOM 2444 C ASP A 8389.738 −8.838 27.723 1.00 27.26 ATOM 2445 O ASP A 838 9.570 −7.716 28.2021.00 27.48 ATOM 2446 N CYS A 839 8.740 −9.550 27.207 1.00 26.97 ATOM2447 CA CYS A 839 7.372 −9.035 27.207 1.00 26.65 ATOM 2448 CB CYS A 8396.668 −9.360 25.882 1.00 26.64 ATOM 2449 SG CYS A 839 7.139 −8.30124.485 1.00 26.65 ATOM 2450 C CYS A 839 6.586 −9.638 28.365 1.00 27.57ATOM 2451 O CYS A 839 5.373 −9.461 28.471 1.00 26.86 ATOM 2452 N PHE A840 7.282 −10.352 29.243 1.00 26.10 ATOM 2453 CA PHE A 840 6.626 −10.97630.385 1.00 26.52 ATOM 2454 CB PHE A 840 7.653 −11.679 31.281 1.00 35.43ATOM 2455 CG PHE A 840 7.045 −12.344 32.485 1.00 35.52 ATOM 2456 CD1 PHEA 840 6.211 −13.450 32.340 1.00 35.69 ATOM 2457 CD2 PHE A 840 7.273−11.842 33.762 1.00 35.56 ATOM 2458 CE1 PHE A 840 5.610 −14.046 33.4501.00 35.99 ATOM 2459 CE2 PHE A 840 6.678 −12.429 34.878 1.00 35.60 ATOM2460 CZ PHE A 840 5.843 −13.533 34.722 1.00 35.62 ATOM 2461 C PHE A 8405.810 −9.991 31.227 1.00 25.53 ATOM 2462 O PHE A 840 4.726 −10.33231.698 1.00 26.75 ATOM 2463 N PRO A 841 6.311 −8.757 31.422 1.00 24.00ATOM 2464 CD PRO A 841 7.585 −8.177 30.965 1.00 27.23 ATOM 2465 CA PRO A841 5.567 −7.783 32.225 1.00 23.95 ATOM 2466 CB PRO A 841 6.345 −6.49132.002 1.00 26.33 ATOM 2467 CG PRO A 841 7.751 −6.988 31.890 1.00 27.03ATOM 2468 C PRO A 841 4.104 −7.662 31.821 1.00 24.02 ATOM 2469 O PRO A841 3.238 −7.446 32.667 1.00 23.76 ATOM 2470 N LEU A 842 3.826 −7.80930.531 1.00 23.41 ATOM 2471 CA LEU A 842 2.447 −7.711 30.069 1.00 22.32ATOM 2472 CB LEU A 842 2.400 −7.647 28.540 1.00 22.25 ATOM 2473 CG LEU A842 3.064 −6.397 27.957 1.00 22.19 ATOM 2474 CD1 LEU A 842 3.184 −6.52726.442 1.00 21.97 ATOM 2475 CD2 LEU A 842 2.255 −5.154 28.349 1.00 23.44ATOM 2476 C LEU A 842 1.633 −8.888 30.590 1.00 23.15 ATOM 2477 O LEU A842 0.508 −8.714 31.048 1.00 22.28 ATOM 2478 N LEU A 843 2.210 −10.08530.537 1.00 20.37 ATOM 2479 CA LEU A 843 1.528 −11.277 31.019 1.00 22.54ATOM 2480 CB LEU A 843 2.369 −12.517 30.716 1.00 30.62 ATOM 2481 CG LEUA 843 1.666 −13.867 30.542 1.00 32.10 ATOM 2482 CD1 LEU A 843 2.718−14.960 30.647 1.00 31.42 ATOM 2483 CD2 LEU A 843 0.586 −14.078 31.5791.00 31.97 ATOM 2484 C LEU A 843 1.338 −11.162 32.531 1.00 20.83 ATOM2485 O LEU A 843 0.252 −11.406 33.057 1.00 22.49 ATOM 2486 N ASP A 8442.410 −10.791 33.222 1.00 25.10 ATOM 2487 CA ASP A 844 2.381 −10.65034.673 1.00 25.84 ATOM 2488 CB ASP A 844 3.756 −10.204 35.177 1.00 33.41ATOM 2489 CG ASP A 844 3.889 −10.316 36.680 1.00 33.77 ATOM 2490 OD1 ASPA 844 3.499 −11.367 37.233 1.00 33.62 ATOM 2491 OD2 ASP A 844 4.392−9.360 37.305 1.00 34.08 ATOM 2492 C ASP A 844 1.306 −9.667 35.129 1.0025.11 ATOM 2493 O ASP A 844 0.517 −9.976 36.020 1.00 25.50 ATOM 2494 NGLY A 845 1.272 −8.492 34.505 1.00 23.99 ATOM 2495 CA GLY A 845 0.282−7.488 34.861 1.00 24.47 ATOM 2496 C GLY A 845 −1.141 −7.954 34.612 1.0024.36 ATOM 2497 O GLY A 845 −2.057 −7.628 35.366 1.00 23.75 ATOM 2498 NCYS A 846 −1.325 −8.720 33.542 1.00 23.31 ATOM 2499 CA CYS A 846 −2.631−9.252 33.188 1.00 22.27 ATOM 2500 CB CYS A 846 −2.556 −9.961 31.8331.00 24.57 ATOM 2501 SG CYS A 846 −4.118 −10.668 31.278 1.00 23.77 ATOM2502 C CYS A 846 −3.093 −10.236 34.255 1.00 23.19 ATOM 2503 O CYS A 846−4.237 −10.197 34.699 1.00 23.71 ATOM 2504 N ARG A 847 −2.197 −11.12634.669 1.00 25.45 ATOM 2505 CA ARG A 847 −2.554 −12.103 35.681 1.0026.33 ATOM 2506 CB ARG A 847 −1.454 −13.170 35.788 1.00 44.92 ATOM 2507CG ARG A 847 −1.334 −13.973 34.489 1.00 45.65 ATOM 2508 CD ARG A 847−0.520 −15.257 34.590 1.00 45.89 ATOM 2509 NE ARG A 847 0.924 −15.03734.557 1.00 45.99 ATOM 2510 CZ ARG A 847 1.805 −15.950 34.155 1.00 45.73ATOM 2511 NH1 ARG A 847 1.392 −17.142 33.743 1.00 45.92 ATOM 2512 NH2ARG A 847 3.102 −15.678 34.178 1.00 45.71 ATOM 2513 C ARG A 847 −2.839−11.434 37.021 1.00 25.65 ATOM 2514 O ARG A 847 −3.673 −11.909 37.7941.00 25.84 ATOM 2515 N LYS A 848 −2.172 −10.319 37.291 1.00 27.18 ATOM2516 CA LYS A 848 −2.408 −9.606 38.540 1.00 27.41 ATOM 2517 CB LYS A 848−1.344 −8.529 38.755 1.00 29.68 ATOM 2518 CG LYS A 848 0.011 −9.08239.165 1.00 30.06 ATOM 2519 CD LYS A 848 1.023 −7.964 39.328 1.00 30.03ATOM 2520 CE LYS A 848 2.406 −8.518 39.644 1.00 30.39 ATOM 2521 NZ LYS A848 3.450 −7.453 39.583 1.00 30.98 ATOM 2522 C LYS A 848 −3.796 −8.97438.514 1.00 27.81 ATOM 2523 O LYS A 848 −4.515 −8.996 39.511 1.00 28.26ATOM 2524 N ASN A 849 −4.179 −8.412 37.372 1.00 28.20 ATOM 2525 CA ASN A849 −5.498 −7.807 37.270 1.00 26.64 ATOM 2526 CB ASN A 849 −5.640 −7.02835.961 1.00 26.08 ATOM 2527 CG ASN A 849 −4.970 −5.674 36.027 1.00 25.73ATOM 2528 OD1 ASN A 849 −4.993 −5.012 37.067 1.00 26.13 ATOM 2529 ND2ASN A 849 −4.382 −5.247 34.923 1.00 26.48 ATOM 2530 C ASN A 849 −6.572−8.875 37.372 1.00 27.18 ATOM 2531 O ASN A 849 −7.679 −8.612 37.844 1.0026.84 ATOM 2532 N ARG A 850 −6.244 −10.086 36.934 1.00 25.96 ATOM 2533CA ARG A 850 −7.194 −11.177 37.017 1.00 26.10 ATOM 2534 CB ARG A 850−6.640 −12.431 36.338 1.00 38.03 ATOM 2535 CG ARG A 850 −7.583 −13.60736.453 1.00 38.77 ATOM 2536 CD ARG A 850 −6.976 −14.898 35.941 1.0038.89 ATOM 2537 NE ARG A 850 −7.798 −16.037 36.336 1.00 39.62 ATOM 2538CZ ARG A 850 −9.075 −16.181 36.003 1.00 39.00 ATOM 2539 NH1 ARG A 850−9.669 −15.255 35.264 1.00 40.11 ATOM 2540 NH2 ARG A 850 −9.765 −17.23536.417 1.00 38.97 ATOM 2541 C ARG A 850 −7.513 −11.488 38.480 1.00 25.71ATOM 2542 O ARG A 850 −8.675 −11.647 38.849 1.00 26.96 ATOM 2543 N GLN A851 −6.476 −11.564 39.311 1.00 29.93 ATOM 2544 CA GLN A 851 −6.659−11.860 40.728 1.00 30.30 ATOM 2545 CB GLN A 851 −5.294 −11.993 41.4131.00 53.42 ATOM 2546 CG GLN A 851 −4.938 −10.873 42.375 1.00 54.29 ATOM2547 CD GLN A 851 −3.479 −10.910 42.794 1.00 54.54 ATOM 2548 OE1 GLN A851 −3.071 −10.204 43.717 1.00 54.48 ATOM 2549 NE2 GLN A 851 −2.681−11.724 42.106 1.00 54.48 ATOM 2550 C GLN A 851 −7.493 −10.765 41.3811.00 29.94 ATOM 2551 O GLN A 851 −8.377 −11.042 42.189 1.00 30.04 ATOM2552 N LYS A 852 −7.213 −9.518 41.017 1.00 27.54 ATOM 2553 CA LYS A 852−7.950 −8.381 41.557 1.00 27.65 ATOM 2554 CB LYS A 852 −7.378 −7.07540.998 1.00 40.34 ATOM 2555 CG LYS A 852 −6.005 −6.705 41.527 1.00 40.79ATOM 2556 CD LYS A 852 −6.096 −6.263 42.977 1.00 40.88 ATOM 2557 CE LYSA 852 −4.760 −5.766 43.497 1.00 40.95 ATOM 2558 NZ LYS A 852 −4.883−5.208 44.879 1.00 41.45 ATOM 2559 C LYS A 852 −9.433 −8.470 41.204 1.0027.70 ATOM 2560 O LYS A 852 −10.301 −8.360 42.075 1.00 27.95 ATOM 2561 NTRP A 853 −9.722 −8.655 39.920 1.00 24.75 ATOM 2562 CA TRP A 853 −11.103−8.747 39.467 1.00 25.36 ATOM 2563 CB TRP A 853 −11.150 −8.857 37.9401.00 23.18 ATOM 2564 CG TRP A 853 −10.967 −7.544 37.240 1.00 23.11 ATOM2565 CD2 TRP A 853 −11.771 −6.368 37.399 1.00 22.95 ATOM 2566 CE2 TRP A853 −11.244 −5.382 36.534 1.00 22.63 ATOM 2567 CE3 TRP A 853 −12.886−6.052 38.189 1.00 23.00 ATOM 2568 CD1 TRP A 853 −10.013 −7.233 36.3121.00 23.06 ATOM 2569 NE1 TRP A 853 −10.173 −5.937 35.884 1.00 22.64 ATOM2570 CZ2 TRP A 853 −11.794 −4.101 36.436 1.00 22.97 ATOM 2571 CZ3 TRP A853 −13.433 −4.778 38.092 1.00 22.86 ATOM 2572 CH2 TRP A 853 −12.886−3.818 37.220 1.00 22.99 ATOM 2573 C TRP A 853 −11.816 −9.931 40.1011.00 24.85 ATOM 2574 O TRP A 853 −12.976 −9.824 40.505 1.00 24.94 ATOM2575 N GLN A 854 −11.107 −11.051 40.202 1.00 28.90 ATOM 2576 CA GLN A854 −11.662 −12.264 40.785 1.00 30.44 ATOM 2577 CB GLN A 854 −10.673−13.419 40.625 1.00 37.29 ATOM 2578 CG GLN A 854 −11.183 −14.749 41.1521.00 37.88 ATOM 2579 CD GLN A 854 −12.554 −15.102 40.608 1.00 38.02 ATOM2580 OE1 GLN A 854 −12.812 −14.978 39.411 1.00 38.44 ATOM 2581 NE2 GLN A854 −13.439 −15.557 41.487 1.00 38.37 ATOM 2582 C GLN A 854 −12.014−12.081 42.257 1.00 30.52 ATOM 2583 O GLN A 854 −12.994 −12.650 42.7361.00 31.44 ATOM 2584 N ALA A 855 −11.219 −11.288 42.969 1.00 32.15 ATOM2585 CA ALA A 855 −11.465 −11.039 44.388 1.00 32.96 ATOM 2586 CB ALA A855 −10.282 −10.300 45.003 1.00 27.28 ATOM 2587 C ALA A 855 −12.747−10.231 44.572 1.00 33.38 ATOM 2588 O ALA A 855 −13.473 −10.411 45.5511.00 33.79 ATOM 2589 N LEU A 856 −13.020 −9.338 43.627 1.00 34.25 ATOM2590 CA LEU A 856 −14.223 −8.517 43.685 1.00 34.81 ATOM 2591 CB LEU A856 −14.102 −7.325 42.732 1.00 29.75 ATOM 2592 CG LEU A 856 −12.988−6.310 43.001 1.00 29.61 ATOM 2593 CD1 LEU A 856 −12.998 −5.251 41.9261.00 29.93 ATOM 2594 CD2 LEU A 856 −13.180 −5.679 44.373 1.00 29.63 ATOM2595 C LEU A 856 −15.455 −9.339 43.315 1.00 35.51 ATOM 2596 O LEU A 856−16.560 −9.063 43.786 1.00 35.20 ATOM 2597 N ALA A 857 −15.258 −10.35842.484 1.00 39.71 ATOM 2598 CA ALA A 857 −16.354 −11.208 42.030 1.0040.78 ATOM 2599 CB ALA A 857 −16.044 −11.745 40.640 1.00 32.69 ATOM 2600C ALA A 857 −16.710 −12.369 42.956 1.00 41.78 ATOM 2601 O ALA A 857−17.849 −12.833 42.951 1.00 41.70 ATOM 2602 N GLU A 858 −15.748 −12.84743.738 1.00 51.08 ATOM 2603 CA GLU A 858 −16.005 −13.967 44.639 1.0052.63 ATOM 2604 CB GLU A 858 −14.710 −14.741 44.909 1.00 56.18 ATOM 2605CG GLU A 858 −13.570 −13.890 45.433 1.00 56.32 ATOM 2606 CD GLU A 858−12.341 −14.710 45.778 1.00 56.60 ATOM 2607 OE1 GLU A 858 −11.844−15.446 44.898 1.00 56.57 ATOM 2608 OE2 GLU A 858 −11.871 −14.614 46.9301.00 56.45 ATOM 2609 C GLU A 858 −16.635 −13.536 45.960 1.00 53.20 ATOM2610 O GLU A 858 −15.986 −13.709 47.014 1.00 53.41 ATOM 2611 OXT GLU A858 −17.776 −13.032 45.927 1.00 56.42 TER ATOM 2613 CB THR B 537 25.25566.687 12.776 1.00 47.44 ATOM 2614 OG1 THR B 537 24.336 67.782 12.8901.00 47.61 ATOM 2615 CG2 THR B 537 25.471 66.356 11.307 1.00 47.41 ATOM2616 C THR B 537 24.866 65.684 15.026 1.00 50.26 ATOM 2617 O THR B 53724.138 65.096 15.828 1.00 50.63 ATOM 2618 N THR B 537 23.266 65.22013.181 1.00 50.23 ATOM 2619 CA THR B 537 24.695 65.462 13.530 1.00 50.15ATOM 2620 N ARG B 538 25.822 66.534 15.395 1.00 48.27 ATOM 2621 CA ARG B538 26.099 66.827 16.801 1.00 48.37 ATOM 2622 CB ARG B 538 24.804 67.21117.532 1.00 55.34 ATOM 2623 CG ARG B 538 24.941 67.437 19.040 1.00 55.68ATOM 2624 CD ARG B 538 25.783 68.664 19.378 1.00 55.76 ATOM 2625 NE ARGB 538 25.806 68.927 20.818 1.00 55.63 ATOM 2626 CZ ARG B 538 26.52969.882 21.401 1.00 55.83 ATOM 2627 NH1 ARG B 538 27.302 70.677 20.6721.00 55.58 ATOM 2628 NH2 ARG B 538 26.481 70.040 22.718 1.00 55.68 ATOM2629 C ARG B 538 26.707 65.579 17.427 1.00 48.47 ATOM 2630 O ARG B 53827.882 65.561 17.796 1.00 47.96 ATOM 2631 N GLU B 539 25.895 64.53417.532 1.00 51.41 ATOM 2632 CA GLU B 539 26.331 63.265 18.096 1.00 50.79ATOM 2633 CB GLU B 539 25.162 62.280 18.093 1.00 45.27 ATOM 2634 CG GLUB 539 25.499 60.877 18.559 1.00 45.43 ATOM 2635 CD GLU B 539 24.27459.985 18.595 1.00 45.09 ATOM 2636 OE1 GLU B 539 23.553 59.931 17.5761.00 45.02 ATOM 2637 OE2 GLU B 539 24.032 59.340 19.636 1.00 45.34 ATOM2638 C GLU B 539 27.490 62.719 17.268 1.00 49.89 ATOM 2639 O GLU B 53928.360 62.015 17.783 1.00 51.14 ATOM 2640 N LEU B 540 27.493 63.05615.981 1.00 35.39 ATOM 2641 CA LEU B 540 28.537 62.617 15.066 1.00 34.61ATOM 2642 CB LEU B 540 28.047 62.729 13.621 1.00 33.85 ATOM 2643 CG LEUB 540 29.094 62.491 12.529 1.00 33.88 ATOM 2644 CD1 LEU B 540 29.75561.135 12.722 1.00 33.93 ATOM 2645 CD2 LEU B 540 28.436 62.579 11.1661.00 34.03 ATOM 2646 C LEU B 540 29.798 63.451 15.245 1.00 33.92 ATOM2647 O LEU B 540 30.910 62.923 15.296 1.00 33.74 ATOM 2648 N GLN B 54129.620 64.763 15.328 1.00 38.91 ATOM 2649 CA GLN B 541 30.747 65.66415.511 1.00 38.96 ATOM 2650 CB GLN B 541 30.265 67.110 15.475 1.00 49.53ATOM 2651 CG GLN B 541 29.654 67.501 14.147 1.00 49.81 ATOM 2652 CD GLNB 541 29.118 68.910 14.156 1.00 49.94 ATOM 2653 OE1 GLN B 541 28.18569.225 14.896 1.00 50.34 ATOM 2654 NE2 GLN B 541 29.707 69.774 13.3361.00 50.07 ATOM 2655 C GLN B 541 31.389 65.356 16.850 1.00 38.55 ATOM2656 O GLN B 541 32.613 65.343 16.980 1.00 39.00 ATOM 2657 N SER B 54230.551 65.099 17.847 1.00 32.80 ATOM 2658 CA SER B 542 31.034 64.77219.177 1.00 32.42 ATOM 2659 CB SER B 542 29.861 64.645 20.153 1.00 41.30ATOM 2660 OG SER B 542 29.144 65.863 20.263 1.00 42.04 ATOM 2661 C SER B542 31.789 63.456 19.113 1.00 30.70 ATOM 2662 O SER B 542 32.848 63.30519.714 1.00 31.49 ATOM 2663 N LEU B 543 31.233 62.505 18.370 1.00 31.05ATOM 2664 CA LEU B 543 31.841 61.188 18.228 1.00 30.13 ATOM 2665 CB LEUB 543 30.895 60.257 17.460 1.00 31.49 ATOM 2666 CG LEU B 543 30.92458.757 17.783 1.00 32.02 ATOM 2667 CD1 LEU B 543 30.315 57.991 16.6151.00 31.51 ATOM 2668 CD2 LEU B 543 32.336 58.278 18.036 1.00 31.28 ATOM2669 C LEU B 543 33.175 61.259 17.492 1.00 29.52 ATOM 2670 O LEU B 54334.183 60.737 17.963 1.00 29.71 ATOM 2671 N ALA B 544 33.175 61.91116.335 1.00 27.41 ATOM 2672 CA ALA B 544 34.374 62.027 15.522 1.00 26.77ATOM 2673 CB ALA B 544 34.040 62.722 14.213 1.00 32.00 ATOM 2674 C ALA B544 35.529 62.748 16.214 1.00 27.56 ATOM 2675 O ALA B 544 36.685 62.35716.075 1.00 27.33 ATOM 2676 N ALA B 545 35.214 63.801 16.960 1.00 29.78ATOM 2677 CA ALA B 545 36.241 64.580 17.642 1.00 29.66 ATOM 2678 CB ALAB 545 35.723 65.990 17.905 1.00 33.66 ATOM 2679 C ALA B 545 36.73163.962 18.948 1.00 30.65 ATOM 2680 O ALA B 545 37.829 64.272 19.417 1.0029.67 ATOM 2681 N ALA B 546 35.921 63.090 19.537 1.00 29.20 ATOM 2682 CAALA B 546 36.284 62.464 20.801 1.00 30.23 ATOM 2683 CB ALA B 546 35.09061.705 21.364 1.00 34.60 ATOM 2684 C ALA B 546 37.493 61.538 20.713 1.0029.49 ATOM 2685 O ALA B 546 37.779 60.959 19.664 1.00 29.95 ATOM 2686 NVAL B 547 38.219 61.423 21.820 1.00 29.24 ATOM 2687 CA VAL B 547 39.37760.543 21.872 1.00 29.27 ATOM 2688 CB VAL B 547 40.359 60.950 22.9901.00 28.05 ATOM 2689 CG1 VAL B 547 41.419 59.877 23.158 1.00 27.67 ATOM2690 CG2 VAL B 547 41.010 62.282 22.650 1.00 28.10 ATOM 2691 C VAL B 54738.845 59.151 22.179 1.00 29.34 ATOM 2692 O VAL B 547 38.009 58.98823.066 1.00 30.26 ATOM 2693 N VAL B 548 39.324 58.152 21.443 1.00 28.29ATOM 2694 CA VAL B 548 38.879 56.778 21.653 1.00 27.44 ATOM 2695 CB VALB 548 38.971 55.953 20.349 1.00 28.22 ATOM 2696 CG1 VAL B 548 38.54554.510 20.613 1.00 27.84 ATOM 2697 CG2 VAL B 548 38.100 56.585 19.2711.00 28.24 ATOM 2698 C VAL B 548 39.721 56.099 22.724 1.00 26.75 ATOM2699 O VAL B 548 40.903 55.822 22.518 1.00 26.81 ATOM 2700 N PRO B 54939.121 55.826 23.890 1.00 24.59 ATOM 2701 CD PRO B 549 37.783 56.26724.317 1.00 25.72 ATOM 2702 CA PRO B 549 39.830 55.172 24.995 1.00 25.08ATOM 2703 CB PRO B 549 38.764 55.089 26.081 1.00 25.73 ATOM 2704 CG PROB 549 37.932 56.312 25.818 1.00 26.01 ATOM 2705 C PRO B 549 40.36253.795 24.600 1.00 26.03 ATOM 2706 O PRO B 549 39.894 53.197 23.628 1.0024.91 ATOM 2707 N SER B 550 41.334 53.298 25.361 1.00 27.34 ATOM 2708 CASER B 550 41.935 51.997 25.088 1.00 27.02 ATOM 2709 CB SER B 550 43.22451.821 25.896 1.00 31.88 ATOM 2710 OG SER B 550 42.943 51.600 27.2671.00 31.82 ATOM 2711 C SER B 550 40.975 50.873 25.440 1.00 26.64 ATOM2712 O SER B 550 40.052 51.062 26.229 1.00 26.84 ATOM 2713 N ALA B 55141.193 49.701 24.853 1.00 26.78 ATOM 2714 CA ALA B 551 40.336 48.55825.135 1.00 27.11 ATOM 2715 CB ALA B 551 40.790 47.342 24.317 1.00 24.60ATOM 2716 C ALA B 551 40.385 48.244 26.630 1.00 27.04 ATOM 2717 O ALA B551 39.373 47.895 27.237 1.00 26.84 ATOM 2718 N GLN B 552 41.573 48.37027.213 1.00 28.38 ATOM 2719 CA GLN B 552 41.775 48.112 28.636 1.00 29.31ATOM 2720 CB GLN B 552 43.233 48.374 29.014 1.00 41.60 ATOM 2721 CG GLNB 552 44.219 47.373 28.448 1.00 42.50 ATOM 2722 CD GLN B 552 45.64647.898 28.453 1.00 42.52 ATOM 2723 OE1 GLN B 552 46.015 48.738 27.6261.00 42.19 ATOM 2724 NE2 GLN B 552 46.453 47.413 29.392 1.00 42.63 ATOM2725 C GLN B 552 40.878 49.011 29.475 1.00 28.87 ATOM 2726 O GLN B 55240.149 48.544 30.355 1.00 28.59 ATOM 2727 N THR B 553 40.944 50.30729.196 1.00 30.11 ATOM 2728 CA THR B 553 40.145 51.283 29.915 1.00 29.74ATOM 2729 CB THR B 553 40.415 52.713 29.399 1.00 32.61 ATOM 2730 OG1 THRB 553 41.795 53.047 29.598 1.00 32.65 ATOM 2731 CG2 THR B 553 39.54153.718 30.142 1.00 32.91 ATOM 2732 C THR B 553 38.655 50.990 29.765 1.0029.20 ATOM 2733 O THR B 553 37.919 50.996 30.747 1.00 29.52 ATOM 2734 NLEU B 554 38.225 50.723 28.534 1.00 27.01 ATOM 2735 CA LEU B 554 36.82050.455 28.244 1.00 26.50 ATOM 2736 CB LEU B 554 36.562 50.590 26.7411.00 28.84 ATOM 2737 CG LEU B 554 36.851 51.973 26.146 1.00 29.16 ATOM2738 CD1 LEU B 554 36.766 51.908 24.630 1.00 29.33 ATOM 2739 CD2 LEU B554 35.862 52.992 26.699 1.00 29.62 ATOM 2740 C LEU B 554 36.324 49.09828.733 1.00 26.37 ATOM 2741 O LEU B 554 35.117 48.879 28.832 1.00 26.37ATOM 2742 N LYS B 555 37.255 48.192 29.026 1.00 25.28 ATOM 2743 CA LYS B555 36.931 46.857 29.524 1.00 24.39 ATOM 2744 CB LYS B 555 36.089 46.95830.802 1.00 35.97 ATOM 2745 CG LYS B 555 36.740 47.722 31.945 1.00 36.48ATOM 2746 CD LYS B 555 35.806 47.781 33.150 1.00 36.95 ATOM 2747 CE LYSB 555 36.409 48.579 34.297 1.00 36.81 ATOM 2748 NZ LYS B 555 35.49948.633 35.478 1.00 37.17 ATOM 2749 C LYS B 555 36.188 45.975 28.520 1.0024.71 ATOM 2750 O LYS B 555 35.592 44.966 28.905 1.00 24.80 ATOM 2751 NILE B 556 36.229 46.336 27.242 1.00 24.43 ATOM 2752 CA ILE B 556 35.52045.556 26.231 1.00 24.37 ATOM 2753 CB ILE B 556 35.436 46.312 24.8951.00 23.67 ATOM 2754 CG2 ILE B 556 34.651 47.601 25.078 1.00 24.41 ATOM2755 CG1 ILE B 556 36.838 46.637 24.384 1.00 24.28 ATOM 2756 CD1 ILE B556 36.847 47.138 22.956 1.00 23.53 ATOM 2757 C ILE B 556 36.095 44.16725.966 1.00 23.99 ATOM 2758 O ILE B 556 35.499 43.380 25.235 1.00 23.82ATOM 2759 N THR B 557 37.246 43.860 26.551 1.00 24.82 ATOM 2760 CA THR B557 37.843 42.545 26.345 1.00 25.70 ATOM 2761 CB THR B 557 39.381 42.59326.486 1.00 34.81 ATOM 2762 OG1 THR B 557 39.901 43.678 25.706 1.0034.99 ATOM 2763 CG2 THR B 557 40.001 41.289 25.991 1.00 34.84 ATOM 2764C THR B 557 37.289 41.526 27.344 1.00 25.75 ATOM 2765 O THR B 557 37.42540.318 27.154 1.00 25.95 ATOM 2766 N ASP B 558 36.646 42.013 28.400 1.0021.17 ATOM 2767 CA ASP B 558 36.099 41.126 29.423 1.00 20.89 ATOM 2768CB ASP B 558 35.952 41.873 30.750 1.00 39.26 ATOM 2769 CG ASP B 55837.214 42.607 31.147 1.00 40.04 ATOM 2770 OD1 ASP B 558 38.293 41.98131.148 1.00 40.44 ATOM 2771 OD2 ASP B 558 37.124 43.809 31.464 1.0040.62 ATOM 2772 C ASP B 558 34.742 40.543 29.045 1.00 21.50 ATOM 2773 OASP B 558 33.846 41.259 28.594 1.00 21.10 ATOM 2774 N PHE B 559 34.58639.242 29.246 1.00 27.65 ATOM 2775 CA PHE B 559 33.322 38.583 28.9421.00 28.56 ATOM 2776 CB PHE B 559 33.474 37.067 29.076 1.00 27.72 ATOM2777 CG PHE B 559 34.269 36.438 27.968 1.00 27.53 ATOM 2778 CD1 PHE B559 33.773 36.407 26.670 1.00 27.89 ATOM 2779 CD2 PHE B 559 35.50935.863 28.224 1.00 27.40 ATOM 2780 CE1 PHE B 559 34.499 35.809 25.6421.00 27.88 ATOM 2781 CE2 PHE B 559 36.243 35.263 27.202 1.00 27.42 ATOM2782 CZ PHE B 559 35.738 35.236 25.911 1.00 27.16 ATOM 2783 C PHE B 55932.214 39.072 29.872 1.00 28.90 ATOM 2784 O PHE B 559 31.030 38.98329.545 1.00 28.49 ATOM 2785 N SER B 560 32.604 39.597 31.029 1.00 29.75ATOM 2786 CA SER B 560 31.638 40.087 32.008 1.00 30.25 ATOM 2787 CB SERB 560 32.204 39.924 33.421 1.00 41.19 ATOM 2788 OG SER B 560 33.40840.654 33.576 1.00 41.28 ATOM 2789 C SER B 560 31.248 41.543 31.778 1.0030.07 ATOM 2790 O SER B 560 30.571 42.149 32.609 1.00 29.90 ATOM 2791 NPHE B 561 31.674 42.098 30.648 1.00 25.27 ATOM 2792 CA PHE B 561 31.37743.484 30.297 1.00 24.91 ATOM 2793 CB PHE B 561 31.775 43.744 28.8421.00 26.48 ATOM 2794 CG PHE B 561 31.458 45.135 28.357 1.00 26.42 ATOM2795 CD1 PHE B 561 32.349 46.181 28.564 1.00 26.47 ATOM 2796 CD2 PHE B561 30.267 45.392 27.679 1.00 26.27 ATOM 2797 CE1 PHE B 561 32.06147.468 28.100 1.00 27.33 ATOM 2798 CE2 PHE B 561 29.970 46.676 27.2101.00 26.55 ATOM 2799 CZ PHE B 561 30.870 47.715 27.421 1.00 26.39 ATOM2800 C PHE B 561 29.904 43.837 30.476 1.00 24.69 ATOM 2801 O PHE B 56129.020 43.040 30.170 1.00 25.07 ATOM 2802 N SER B 562 29.652 45.04730.966 1.00 26.30 ATOM 2803 CA SER B 562 28.291 45.538 31.163 1.00 27.46ATOM 2804 CB SER B 562 27.992 45.694 32.655 1.00 44.74 ATOM 2805 OG SERB 562 26.657 46.118 32.861 1.00 45.35 ATOM 2806 C SER B 562 28.18846.895 30.476 1.00 25.80 ATOM 2807 O SER B 562 29.092 47.721 30.593 1.0025.80 ATOM 2808 N ASP B 563 27.094 47.120 29.756 1.00 22.70 ATOM 2809 CAASP B 563 26.896 48.380 29.050 1.00 23.18 ATOM 2810 CB ASP B 563 26.20348.138 27.709 1.00 23.75 ATOM 2811 CG ASP B 563 24.700 47.931 27.8611.00 23.45 ATOM 2812 OD1 ASP B 563 24.282 46.853 28.330 1.00 23.97 ATOM2813 OD2 ASP B 563 23.936 48.858 27.522 1.00 24.26 ATOM 2814 C ASP B 56326.014 49.330 29.847 1.00 22.69 ATOM 2815 O ASP B 563 25.889 50.50429.503 1.00 23.59 ATOM 2816 N PHE B 564 25.398 48.813 30.902 1.00 25.43ATOM 2817 CA PHE B 564 24.471 49.599 31.708 1.00 26.75 ATOM 2818 CB PHEB 564 24.056 48.800 32.942 1.00 37.63 ATOM 2819 CG PHE B 564 22.81749.324 33.606 1.00 38.09 ATOM 2820 CD1 PHE B 564 21.604 49.337 32.9211.00 38.40 ATOM 2821 CD2 PHE B 564 22.858 49.809 34.907 1.00 38.36 ATOM2822 CE1 PHE B 564 20.446 49.826 33.525 1.00 38.54 ATOM 2823 CE2 PHE B564 21.706 50.301 35.522 1.00 38.90 ATOM 2824 CZ PHE B 564 20.498 50.30934.829 1.00 38.44 ATOM 2825 C PHE B 564 24.907 50.999 32.137 1.00 27.15ATOM 2826 O PHE B 564 24.118 51.945 32.064 1.00 26.92 ATOM 2827 N GLU B565 26.156 51.139 32.566 1.00 29.91 ATOM 2828 CA GLU B 565 26.654 52.43133.034 1.00 30.93 ATOM 2829 CB GLU B 565 27.762 52.219 34.069 1.00 40.08ATOM 2830 CG GLU B 565 27.372 51.367 35.270 1.00 40.03 ATOM 2831 CD GLUB 565 27.050 49.935 34.890 1.00 40.48 ATOM 2832 OE1 GLU B 565 27.78749.363 34.058 1.00 40.51 ATOM 2833 OE2 GLU B 565 26.066 49.378 35.4281.00 40.01 ATOM 2834 C GLU B 565 27.173 53.361 31.944 1.00 30.09 ATOM2835 O GLU B 565 27.567 54.497 32.227 1.00 30.95 ATOM 2836 N LEU B 56627.167 52.894 30.700 1.00 27.08 ATOM 2837 CA LEU B 566 27.671 53.69229.594 1.00 26.42 ATOM 2838 CB LEU B 566 28.395 52.784 28.591 1.00 35.46ATOM 2839 CG LEU B 566 29.522 51.884 29.106 1.00 36.46 ATOM 2840 CD1 LEUB 566 30.022 50.996 27.969 1.00 35.95 ATOM 2841 CD2 LEU B 566 30.65952.730 29.659 1.00 36.32 ATOM 2842 C LEU B 566 26.600 54.483 28.860 1.0025.95 ATOM 2843 O LEU B 566 25.454 54.048 28.756 1.00 24.61 ATOM 2844 NSER B 567 26.986 55.655 28.358 1.00 25.45 ATOM 2845 CA SER B 567 26.08056.501 27.590 1.00 25.56 ATOM 2846 CB SER B 567 26.519 57.963 27.6651.00 33.98 ATOM 2847 OG SER B 567 27.722 58.173 26.947 1.00 34.14 ATOM2848 C SER B 567 26.155 56.027 26.140 1.00 25.50 ATOM 2849 O SER B 56727.047 55.247 25.791 1.00 23.97 ATOM 2850 N ASP B 568 25.234 56.49025.300 1.00 26.74 ATOM 2851 CA ASP B 568 25.240 56.101 23.892 1.00 26.93ATOM 2852 CB ASP B 568 24.110 56.790 23.127 1.00 31.14 ATOM 2853 CG ASPB 568 22.760 56.161 23.390 1.00 31.71 ATOM 2854 OD1 ASP B 568 21.78356.584 22.743 1.00 32.07 ATOM 2855 OD2 ASP B 568 22.678 55.246 24.2401.00 31.51 ATOM 2856 C ASP B 568 26.569 56.455 23.241 1.00 26.60 ATOM2857 O ASP B 568 27.130 55.656 22.494 1.00 26.36 ATOM 2858 N LEU B 56927.071 57.656 23.526 1.00 26.00 ATOM 2859 CA LEU B 569 28.341 58.09122.964 1.00 25.02 ATOM 2860 CB LEU B 569 28.683 59.507 23.446 1.00 35.36ATOM 2861 CG LEU B 569 30.009 60.124 22.980 1.00 35.65 ATOM 2862 CD1 LEUB 569 30.050 60.203 21.464 1.00 36.29 ATOM 2863 CD2 LEU B 569 30.15361.516 23.583 1.00 35.93 ATOM 2864 C LEU B 569 29.432 57.113 23.388 1.0024.35 ATOM 2865 O LEU B 569 30.267 56.716 22.574 1.00 25.31 ATOM 2866 NGLU B 570 29.412 56.715 24.659 1.00 23.22 ATOM 2867 CA GLU B 570 30.40655.784 25.173 1.00 23.38 ATOM 2868 CB GLU B 570 30.216 55.560 26.6761.00 33.69 ATOM 2869 CG GLU B 570 30.567 56.787 27.522 1.00 34.19 ATOM2870 CD GLU B 570 30.543 56.509 29.017 1.00 34.09 ATOM 2871 OE1 GLU B570 29.467 56.160 29.548 1.00 33.38 ATOM 2872 OE2 GLU B 570 31.60556.642 29.665 1.00 35.27 ATOM 2873 C GLU B 570 30.351 54.458 24.423 1.0023.12 ATOM 2874 O GLU B 570 31.397 53.899 24.085 1.00 23.04 ATOM 2875 NTHR B 571 29.148 53.954 24.155 1.00 23.20 ATOM 2876 CA THR B 571 29.03852.692 23.423 1.00 23.72 ATOM 2877 CB THR B 571 27.582 52.146 23.3671.00 22.43 ATOM 2878 OG1 THR B 571 26.753 53.014 22.589 1.00 23.16 ATOM2879 CG2 THR B 571 27.010 52.013 24.772 1.00 23.40 ATOM 2880 C THR B 57129.564 52.865 22.000 1.00 22.59 ATOM 2881 O THR B 571 30.147 51.93721.441 1.00 23.35 ATOM 2882 N ALA B 572 29.367 54.047 21.418 1.00 23.15ATOM 2883 CA ALA B 572 29.852 54.323 20.065 1.00 23.02 ATOM 2884 CB ALAB 572 29.330 55.671 19.575 1.00 25.21 ATOM 2885 C ALA B 572 31.38154.315 20.061 1.00 24.49 ATOM 2886 O ALA B 572 32.007 53.797 19.133 1.0023.72 ATOM 2887 N LEU B 573 31.984 54.906 21.092 1.00 24.96 ATOM 2888 CALEU B 573 33.438 54.924 21.203 1.00 25.56 ATOM 2889 CB LEU B 573 33.87055.787 22.395 1.00 25.61 ATOM 2890 CG LEU B 573 33.684 57.294 22.2041.00 25.96 ATOM 2891 CD1 LEU B 573 33.998 58.025 23.505 1.00 25.46 ATOM2892 CD2 LEU B 573 34.581 57.784 21.076 1.00 24.77 ATOM 2893 C LEU B 57333.961 53.490 21.363 1.00 23.87 ATOM 2894 O LEU B 573 34.960 53.11620.744 1.00 25.16 ATOM 2895 N CYS B 574 33.291 52.697 22.195 1.00 21.17ATOM 2896 CA CYS B 574 33.672 51.297 22.406 1.00 20.66 ATOM 2897 CB CYSB 574 32.687 50.593 23.342 1.00 22.74 ATOM 2898 SG CYS B 574 32.88250.908 25.120 1.00 21.69 ATOM 2899 C CYS B 574 33.665 50.555 21.072 1.0021.23 ATOM 2900 O CYS B 574 34.536 49.727 20.801 1.00 19.77 ATOM 2901 NTHR B 575 32.668 50.849 20.248 1.00 21.05 ATOM 2902 CA THR B 575 32.54350.203 18.948 1.00 20.83 ATOM 2903 CB THR B 575 31.211 50.590 18.2731.00 21.54 ATOM 2904 OG1 THR B 575 30.128 50.166 19.109 1.00 22.40 ATOM2905 CG2 THR B 575 31.067 49.917 16.912 1.00 22.61 ATOM 2906 C THR B 57533.722 50.565 18.052 1.00 21.63 ATOM 2907 O THR B 575 34.268 49.70817.357 1.00 20.92 ATOM 2908 N ILE B 576 34.122 51.833 18.068 1.00 21.26ATOM 2909 CA ILE B 576 35.256 52.261 17.254 1.00 21.61 ATOM 2910 CB ILEB 576 35.510 53.786 17.365 1.00 24.97 ATOM 2911 CG2 ILE B 576 36.81754.147 16.660 1.00 25.32 ATOM 2912 CG1 ILE B 576 34.333 54.558 16.7571.00 25.33 ATOM 2913 CD1 ILE B 576 34.503 56.083 16.761 1.00 25.78 ATOM2914 C ILE B 576 36.506 51.521 17.717 1.00 22.18 ATOM 2915 O ILE B 57637.344 51.139 16.900 1.00 21.36 ATOM 2916 N ARG B 577 36.619 51.31819.028 1.00 21.36 ATOM 2917 CA ARG B 577 37.761 50.620 19.598 1.00 22.50ATOM 2918 CB ARG B 577 37.749 50.702 21.131 1.00 20.87 ATOM 2919 CG ARGB 577 38.879 49.924 21.796 1.00 21.90 ATOM 2920 CD ARG B 577 40.23950.280 21.195 1.00 21.96 ATOM 2921 NE ARG B 577 40.657 51.648 21.5011.00 21.18 ATOM 2922 CZ ARG B 577 41.693 52.255 20.927 1.00 22.44 ATOM2923 NH1 ARG B 577 42.421 51.622 20.011 1.00 22.46 ATOM 2924 NH2 ARG B577 42.005 53.504 21.265 1.00 22.38 ATOM 2925 C ARG B 577 37.779 49.16419.149 1.00 21.04 ATOM 2926 O ARG B 577 38.846 48.599 18.938 1.00 23.18ATOM 2927 N MET B 578 36.600 48.560 19.000 1.00 21.91 ATOM 2928 CA MET B578 36.507 47.172 18.548 1.00 21.13 ATOM 2929 CB MET B 578 35.054 46.70518.554 1.00 20.87 ATOM 2930 CG MET B 578 34.503 46.404 19.925 1.00 21.65ATOM 2931 SD MET B 578 32.749 46.041 19.841 1.00 22.25 ATOM 2932 CE METB 578 32.205 46.673 21.420 1.00 22.99 ATOM 2933 C MET B 578 37.07947.018 17.135 1.00 21.37 ATOM 2934 O MET B 578 37.872 46.114 16.876 1.0021.93 ATOM 2935 N PHE B 579 36.660 47.886 16.222 1.00 21.44 ATOM 2936 CAPHE B 579 37.160 47.840 14.850 1.00 20.75 ATOM 2937 CB PHE B 579 36.49648.908 13.979 1.00 23.89 ATOM 2938 CG PHE B 579 35.160 48.512 13.4401.00 22.77 ATOM 2939 CD1 PHE B 579 34.009 48.672 14.203 1.00 22.94 ATOM2940 CD2 PHE B 579 35.051 47.979 12.161 1.00 22.86 ATOM 2941 CE1 PHE B579 32.765 48.302 13.695 1.00 23.49 ATOM 2942 CE2 PHE B 579 33.81347.607 11.645 1.00 23.55 ATOM 2943 CZ PHE B 579 32.668 47.769 12.4151.00 23.73 ATOM 2944 C PHE B 579 38.660 48.101 14.832 1.00 21.82 ATOM2945 O PHE B 579 39.411 47.442 14.113 1.00 20.97 ATOM 2946 N THR B 58039.085 49.074 15.628 1.00 23.77 ATOM 2947 CA THR B 580 40.488 49.45015.684 1.00 23.88 ATOM 2948 CB THR B 580 40.684 50.693 16.572 1.00 24.40ATOM 2949 OG1 THR B 580 39.895 51.770 16.051 1.00 25.13 ATOM 2950 CG2THR B 580 42.153 51.109 16.596 1.00 24.68 ATOM 2951 C THR B 580 41.40248.338 16.174 1.00 24.19 ATOM 2952 O THR B 580 42.389 48.011 15.512 1.0024.60 ATOM 2953 N ASP B 581 41.072 47.743 17.314 1.00 26.39 ATOM 2954 CAASP B 581 41.903 46.687 17.872 1.00 27.24 ATOM 2955 CB ASP B 581 41.63546.554 19.369 1.00 26.21 ATOM 2956 CG ASP B 581 42.295 47.666 20.1711.00 26.06 ATOM 2957 OD1 ASP B 581 42.688 48.690 19.565 1.00 25.91 ATOM2958 OD2 ASP B 581 42.418 47.520 21.402 1.00 26.26 ATOM 2959 C ASP B 58141.821 45.333 17.182 1.00 27.49 ATOM 2960 O ASP B 581 42.535 44.40317.552 1.00 27.57 ATOM 2961 N LEU B 582 40.947 45.217 16.189 1.00 23.58ATOM 2962 CA LEU B 582 40.859 43.984 15.415 1.00 24.50 ATOM 2963 CB LEUB 582 39.395 43.600 15.139 1.00 22.05 ATOM 2964 CG LEU B 582 38.66042.981 16.337 1.00 21.75 ATOM 2965 CD1 LEU B 582 37.178 42.787 16.0351.00 22.80 ATOM 2966 CD2 LEU B 582 39.309 41.648 16.680 1.00 21.90 ATOM2967 C LEU B 582 41.605 44.305 14.117 1.00 24.79 ATOM 2968 O LEU B 58241.591 43.531 13.153 1.00 25.28 ATOM 2969 N ASN B 583 42.255 45.46914.117 1.00 27.83 ATOM 2970 CA ASN B 583 43.037 45.956 12.984 1.00 30.24ATOM 2971 CB ASN B 583 44.235 45.037 12.740 1.00 52.59 ATOM 2972 CG ASNB 583 45.196 45.017 13.906 1.00 53.50 ATOM 2973 OD1 ASN B 583 44.82744.655 15.023 1.00 53.73 ATOM 2974 ND2 ASN B 583 46.440 45.410 13.6551.00 53.71 ATOM 2975 C ASN B 583 42.223 46.074 11.704 1.00 29.60 ATOM2976 O ASN B 583 42.733 45.818 10.614 1.00 30.55 ATOM 2977 N LEU B 58440.964 46.478 11.840 1.00 27.68 ATOM 2978 CA LEU B 584 40.069 46.62010.696 1.00 27.10 ATOM 2979 CB LEU B 584 38.632 46.323 11.131 1.00 25.59ATOM 2980 CG LEU B 584 38.111 44.884 11.080 1.00 26.48 ATOM 2981 CD1 LEUB 584 39.198 43.891 11.360 1.00 26.71 ATOM 2982 CD2 LEU B 584 36.95444.746 12.065 1.00 24.71 ATOM 2983 C LEU B 584 40.115 47.992 10.047 1.0027.65 ATOM 2984 O LEU B 584 39.908 48.120 8.843 1.00 26.67 ATOM 2985 NVAL B 585 40.380 49.021 10.845 1.00 28.02 ATOM 2986 CA VAL B 585 40.41550.380 10.326 1.00 28.97 ATOM 2987 CB VAL B 585 40.586 51.400 11.4671.00 33.37 ATOM 2988 CG1 VAL B 585 40.639 52.812 10.902 1.00 33.53 ATOM2989 CG2 VAL B 585 39.436 51.267 12.448 1.00 33.91 ATOM 2990 C VAL B 58541.502 50.620 9.283 1.00 29.73 ATOM 2991 O VAL B 585 41.210 51.056 8.1721.00 29.62 ATOM 2992 N GLN B 586 42.749 50.330 9.638 1.00 34.73 ATOM2993 CA GLN B 586 43.860 50.536 8.718 1.00 36.38 ATOM 2994 CB GLN B 58645.171 50.626 9.501 1.00 56.06 ATOM 2995 CG GLN B 586 45.261 51.88710.349 1.00 56.60 ATOM 2996 CD GLN B 586 46.523 51.955 11.184 1.00 57.01ATOM 2997 OE1 GLN B 586 46.729 51.142 12.085 1.00 56.81 ATOM 2998 NE2GLN B 586 47.378 52.930 10.887 1.00 56.83 ATOM 2999 C GLN B 586 43.93649.439 7.666 1.00 35.19 ATOM 3000 O GLN B 586 44.176 49.716 6.492 1.0036.38 ATOM 3001 N ASN B 587 43.716 48.199 8.088 1.00 28.60 ATOM 3002 CAASN B 587 43.749 47.058 7.180 1.00 27.39 ATOM 3003 CB ASN B 587 43.20845.816 7.893 1.00 34.50 ATOM 3004 CG ASN B 587 43.520 44.530 7.155 1.0034.35 ATOM 3005 OD1 ASN B 587 43.721 44.528 5.943 1.00 34.55 ATOM 3006ND2 ASN B 587 43.549 43.423 7.888 1.00 34.96 ATOM 3007 C ASN B 58742.895 47.331 5.941 1.00 27.36 ATOM 3008 O ASN B 587 43.336 47.133 4.8111.00 26.90 ATOM 3009 N PHE B 588 41.666 47.796 6.154 1.00 26.94 ATOM3010 CA PHE B 588 40.765 48.048 5.040 1.00 26.43 ATOM 3011 CB PHE B 58839.423 47.350 5.317 1.00 20.94 ATOM 3012 CG PHE B 588 39.558 45.8565.503 1.00 20.97 ATOM 3013 CD1 PHE B 588 39.472 45.277 6.765 1.00 20.43ATOM 3014 CD2 PHE B 588 39.845 45.038 4.417 1.00 20.60 ATOM 3015 CE1 PHEB 588 39.678 43.899 6.940 1.00 20.54 ATOM 3016 CE2 PHE B 588 40.05243.662 4.576 1.00 19.56 ATOM 3017 CZ PHE B 588 39.969 43.091 5.842 1.0021.12 ATOM 3018 C PHE B 588 40.573 49.521 4.670 1.00 27.33 ATOM 3019 OPHE B 588 39.625 49.878 3.973 1.00 27.04 ATOM 3020 N GLN B 589 41.50250.365 5.111 1.00 28.79 ATOM 3021 CA GLN B 589 41.465 51.800 4.818 1.0029.49 ATOM 3022 CB GLN B 589 41.843 52.064 3.350 1.00 45.46 ATOM 3023 CGGLN B 589 43.334 51.986 3.014 1.00 45.82 ATOM 3024 CD GLN B 589 43.79750.588 2.639 1.00 46.29 ATOM 3025 OE1 GLN B 589 42.993 49.736 2.257 1.0046.04 ATOM 3026 NE2 GLN B 589 45.104 50.353 2.724 1.00 45.90 ATOM 3027 CGLN B 589 40.127 52.481 5.106 1.00 29.77 ATOM 3028 O GLN B 589 39.50953.063 4.212 1.00 29.22 ATOM 3029 N MET B 590 39.686 52.421 6.357 1.0030.86 ATOM 3030 CA MET B 590 38.432 53.050 6.743 1.00 30.28 ATOM 3031 CBMET B 590 37.759 52.259 7.865 1.00 26.11 ATOM 3032 CG MET B 590 37.25450.888 7.485 1.00 26.11 ATOM 3033 SD MET B 590 36.366 50.192 8.891 1.0024.81 ATOM 3034 CE MET B 590 35.005 51.232 8.953 1.00 27.02 ATOM 3035 CMET B 590 38.680 54.467 7.241 1.00 30.44 ATOM 3036 O MET B 590 39.45354.666 8.175 1.00 30.43 ATOM 3037 N LYS B 591 38.039 55.449 6.616 1.0028.66 ATOM 3038 CA LYS B 591 38.181 56.833 7.059 1.00 29.65 ATOM 3039 CBLYS B 591 37.556 57.798 6.045 1.00 48.54 ATOM 3040 CG LYS B 591 38.53058.376 5.022 1.00 49.40 ATOM 3041 CD LYS B 591 39.125 57.314 4.114 1.0049.46 ATOM 3042 CE LYS B 591 40.123 57.925 3.141 1.00 49.63 ATOM 3043 NZLYS B 591 39.519 59.026 2.336 1.00 49.46 ATOM 3044 C LYS B 591 37.45356.951 8.399 1.00 28.39 ATOM 3045 O LYS B 591 36.361 56.409 8.566 1.0028.80 ATOM 3046 N HIS B 592 38.060 57.646 9.354 1.00 26.99 ATOM 3047 CAHIS B 592 37.447 57.803 10.669 1.00 26.60 ATOM 3048 CB HIS B 592 38.30558.713 11.554 1.00 26.53 ATOM 3049 CG HIS B 592 37.869 58.742 12.9851.00 26.27 ATOM 3050 CD2 HIS B 592 37.395 59.750 13.755 1.00 26.34 ATOM3051 ND1 HIS B 592 37.888 57.622 13.788 1.00 26.28 ATOM 3052 CE1 HIS B592 37.446 57.939 14.992 1.00 26.55 ATOM 3053 NE2 HIS B 592 37.14059.224 14.998 1.00 26.20 ATOM 3054 C HIS B 592 36.027 58.366 10.594 1.0026.93 ATOM 3055 O HIS B 592 35.114 57.856 11.244 1.00 26.72 ATOM 3056 NGLU B 593 35.844 59.423 9.810 1.00 25.99 ATOM 3057 CA GLU B 593 34.53260.049 9.675 1.00 26.68 ATOM 3058 CB GLU B 593 34.615 61.240 8.717 1.0047.65 ATOM 3059 CG GLU B 593 35.479 62.386 9.232 1.00 48.65 ATOM 3060 CDGLU B 593 36.880 61.942 9.628 1.00 48.66 ATOM 3061 OE1 GLU B 593 37.59561.373 8.773 1.00 48.66 ATOM 3062 OE2 GLU B 593 37.266 62.160 10.7981.00 48.65 ATOM 3063 C GLU B 593 33.479 59.056 9.188 1.00 25.92 ATOM3064 O GLU B 593 32.368 59.011 9.717 1.00 25.44 ATOM 3065 N VAL B 59433.837 58.257 8.188 1.00 23.11 ATOM 3066 CA VAL B 594 32.914 57.2657.640 1.00 23.96 ATOM 3067 CB VAL B 594 33.511 56.574 6.390 1.00 21.56ATOM 3068 CG1 VAL B 594 32.576 55.471 5.891 1.00 21.95 ATOM 3069 CG2 VALB 594 33.747 57.604 5.297 1.00 21.81 ATOM 3070 C VAL B 594 32.556 56.1968.667 1.00 23.30 ATOM 3071 O VAL B 594 31.385 55.849 8.824 1.00 23.33ATOM 3072 N LEU B 595 33.558 55.663 9.360 1.00 24.80 ATOM 3073 CA LEU B595 33.300 54.639 10.364 1.00 24.45 ATOM 3074 CB LEU B 595 34.616 54.12710.959 1.00 24.30 ATOM 3075 CG LEU B 595 34.502 53.137 12.123 1.00 25.09ATOM 3076 CD1 LEU B 595 33.643 51.938 11.723 1.00 23.72 ATOM 3077 CD2LEU B 595 35.892 52.686 12.545 1.00 23.89 ATOM 3078 C LEU B 595 32.39155.190 11.464 1.00 24.32 ATOM 3079 O LEU B 595 31.482 54.501 11.935 1.0024.28 ATOM 3080 N CYS B 596 32.625 56.437 11.866 1.00 23.70 ATOM 3081 CACYS B 596 31.794 57.057 12.895 1.00 22.77 ATOM 3082 CB CYS B 596 32.35458.426 13.302 1.00 27.45 ATOM 3083 SG CYS B 596 33.875 58.384 14.2771.00 27.23 ATOM 3084 C CYS B 596 30.363 57.233 12.386 1.00 22.78 ATOM3085 O CYS B 596 29.404 56.963 13.108 1.00 22.99 ATOM 3086 N ARG B 59730.221 57.681 11.140 1.00 22.21 ATOM 3087 CA ARG B 597 28.899 57.89310.562 1.00 21.97 ATOM 3088 CB ARG B 597 29.018 58.543 9.178 1.00 33.99ATOM 3089 CG ARG B 597 27.678 58.924 8.570 1.00 35.29 ATOM 3090 CD ARG B597 27.807 59.645 7.228 1.00 35.28 ATOM 3091 NE ARG B 597 28.241 61.0357.362 1.00 35.24 ATOM 3092 CZ ARG B 597 29.494 61.455 7.216 1.00 35.37ATOM 3093 NH1 ARG B 597 30.463 60.596 6.926 1.00 35.79 ATOM 3094 NH2 ARGB 597 29.778 62.745 7.354 1.00 35.68 ATOM 3095 C ARG B 597 28.149 56.56310.459 1.00 21.87 ATOM 3096 O ARG B 597 26.954 56.496 10.729 1.00 21.94ATOM 3097 N TRP B 598 28.862 55.511 10.069 1.00 23.25 ATOM 3098 CA TRP B598 28.264 54.185 9.944 1.00 23.59 ATOM 3099 CB TRP B 598 29.287 53.1949.374 1.00 21.37 ATOM 3100 CG TRP B 598 28.744 51.811 9.234 1.00 19.95ATOM 3101 CD2 TRP B 598 28.905 50.725 10.157 1.00 20.76 ATOM 3102 CE2TRP B 598 28.159 49.636 9.653 1.00 21.16 ATOM 3103 CE3 TRP B 598 29.60250.568 11.363 1.00 20.58 ATOM 3104 CD1 TRP B 598 27.937 51.349 8.2371.00 20.72 ATOM 3105 NE1 TRP B 598 27.581 50.044 8.481 1.00 20.01 ATOM3106 CZ2 TRP B 598 28.091 48.404 10.313 1.00 19.36 ATOM 3107 CZ3 TRP B598 29.534 49.346 12.019 1.00 21.53 ATOM 3108 CH2 TRP B 598 28.78048.277 11.491 1.00 21.51 ATOM 3109 C TRP B 598 27.774 53.687 11.301 1.0023.33 ATOM 3110 O TRP B 598 26.660 53.170 11.429 1.00 22.55 ATOM 3111 NILE B 599 28.614 53.836 12.318 1.00 19.88 ATOM 3112 CA ILE B 599 28.25053.401 13.652 1.00 19.76 ATOM 3113 CB ILE B 599 29.400 53.659 14.6561.00 18.66 ATOM 3114 CG2 ILE B 599 28.917 53.410 16.078 1.00 20.09 ATOM3115 CG1 ILE B 599 30.586 52.742 14.328 1.00 19.91 ATOM 3116 CD1 ILE B599 31.835 53.042 15.140 1.00 18.69 ATOM 3117 C ILE B 599 26.989 54.12414.105 1.00 20.60 ATOM 3118 O ILE B 599 26.072 53.501 14.636 1.00 20.28ATOM 3119 N LEU B 600 26.933 55.435 13.883 1.00 24.36 ATOM 3120 CA LEU B600 25.761 56.200 14.292 1.00 24.27 ATOM 3121 CB LEU B 600 26.023 57.70014.135 1.00 30.88 ATOM 3122 CG LEU B 600 27.104 58.235 15.080 1.00 31.45ATOM 3123 CD1 LEU B 600 27.378 59.680 14.764 1.00 31.56 ATOM 3124 CD2LEU B 600 26.663 58.079 16.529 1.00 31.65 ATOM 3125 C LEU B 600 24.51855.788 13.512 1.00 25.39 ATOM 3126 O LEU B 600 23.432 55.697 14.086 1.0024.82 ATOM 3127 N SER B 601 24.681 55.522 12.216 1.00 24.46 ATOM 3128 CASER B 601 23.563 55.098 11.373 1.00 23.76 ATOM 3129 CB SER B 601 24.01854.931 9.920 1.00 24.34 ATOM 3130 OG SER B 601 24.232 56.181 9.287 1.0024.61 ATOM 3131 C SER B 601 23.004 53.771 11.884 1.00 23.31 ATOM 3132 OSER B 601 21.793 53.574 11.947 1.00 24.08 ATOM 3133 N VAL B 602 23.89552.855 12.248 1.00 20.00 ATOM 3134 CA VAL B 602 23.465 51.560 12.7651.00 19.52 ATOM 3135 CB VAL B 602 24.681 50.622 12.998 1.00 20.56 ATOM3136 CG1 VAL B 602 24.271 49.399 13.806 1.00 20.50 ATOM 3137 CG2 VAL B602 25.258 50.193 11.659 1.00 20.79 ATOM 3138 C VAL B 602 22.685 51.74214.073 1.00 18.74 ATOM 3139 O VAL B 602 21.598 51.188 14.243 1.00 19.51ATOM 3140 N LYS B 603 23.230 52.533 14.989 1.00 21.59 ATOM 3141 CA LYS B603 22.568 52.767 16.268 1.00 22.24 ATOM 3142 CB LYS B 603 23.433 53.67417.156 1.00 32.07 ATOM 3143 CG LYS B 603 22.812 53.968 18.523 1.00 32.67ATOM 3144 CD LYS B 603 23.775 54.700 19.457 1.00 32.26 ATOM 3145 CE LYSB 603 24.152 56.067 18.910 1.00 33.03 ATOM 3146 NZ LYS B 603 24.99156.838 19.866 1.00 33.90 ATOM 3147 C LYS B 603 21.193 53.404 16.072 1.0021.31 ATOM 3148 O LYS B 603 20.229 53.057 16.758 1.00 21.06 ATOM 3149 NLYS B 604 21.103 54.318 15.116 1.00 21.77 ATOM 3150 CA LYS B 604 19.84655.003 14.860 1.00 22.10 ATOM 3151 CB LYS B 604 20.071 56.179 13.9041.00 35.05 ATOM 3152 CG LYS B 604 18.815 56.987 13.614 1.00 35.34 ATOM3153 CD LYS B 604 19.111 58.153 12.691 1.00 35.68 ATOM 3154 CE LYS B 60417.841 58.897 12.313 1.00 35.70 ATOM 3155 NZ LYS B 604 18.118 60.00911.357 1.00 35.94 ATOM 3156 C LYS B 604 18.781 54.088 14.290 1.00 23.45ATOM 3157 O LYS B 604 17.588 54.266 14.567 1.00 23.47 ATOM 3158 N ASN B605 19.200 53.104 13.497 1.00 24.27 ATOM 3159 CA ASN B 605 18.238 52.19812.887 1.00 24.84 ATOM 3160 CB ASN B 605 18.790 51.629 11.580 1.00 33.82ATOM 3161 CG ASN B 605 18.757 52.650 10.461 1.00 34.72 ATOM 3162 OD1 ASNB 605 19.593 53.552 10.401 1.00 35.05 ATOM 3163 ND2 ASN B 605 17.77152.529 9.579 1.00 34.67 ATOM 3164 C ASN B 605 17.713 51.091 13.784 1.0025.28 ATOM 3165 O ASN B 605 17.138 50.109 13.309 1.00 26.57 ATOM 3166 NTYR B 606 17.935 51.237 15.083 1.00 22.80 ATOM 3167 CA TYR B 606 17.38150.301 16.047 1.00 21.47 ATOM 3168 CB TYR B 606 18.406 49.906 17.1161.00 19.39 ATOM 3169 CG TYR B 606 19.259 48.734 16.684 1.00 18.74 ATOM3170 CD1 TYR B 606 20.482 48.930 16.047 1.00 19.52 ATOM 3171 CE1 TYR B606 21.221 47.852 15.566 1.00 19.69 ATOM 3172 CD2 TYR B 606 18.79547.427 16.836 1.00 18.61 ATOM 3173 CE2 TYR B 606 19.530 46.337 16.3551.00 19.30 ATOM 3174 CZ TYR B 606 20.739 46.563 15.719 1.00 19.25 ATOM3175 OH TYR B 606 21.459 45.499 15.209 1.00 18.12 ATOM 3176 C TYR B 60616.234 51.093 16.662 1.00 22.67 ATOM 3177 O TYR B 606 16.323 52.31916.782 1.00 24.05 ATOM 3178 N ARG B 607 15.146 50.419 17.009 1.00 23.34ATOM 3179 CA ARG B 607 13.997 51.106 17.602 1.00 23.02 ATOM 3180 CB ARGB 607 12.718 50.315 17.322 1.00 22.58 ATOM 3181 CG ARG B 607 12.51650.043 15.838 1.00 22.23 ATOM 3182 CD ARG B 607 11.149 49.467 15.5331.00 23.26 ATOM 3183 NE ARG B 607 11.044 49.076 14.131 1.00 21.78 ATOM3184 CZ ARG B 607 9.916 48.698 13.537 1.00 23.35 ATOM 3185 NH1 ARG B 6078.780 48.661 14.220 1.00 22.77 ATOM 3186 NH2 ARG B 607 9.931 48.34412.258 1.00 23.68 ATOM 3187 C ARG B 607 14.247 51.243 19.100 1.00 23.25ATOM 3188 O ARG B 607 14.123 50.282 19.855 1.00 22.89 ATOM 3189 N LYS B608 14.602 52.450 19.526 1.00 26.06 ATOM 3190 CA LYS B 608 14.921 52.69720.928 1.00 27.43 ATOM 3191 CB LYS B 608 15.228 54.183 21.147 1.00 43.34ATOM 3192 CG LYS B 608 14.041 55.104 20.946 1.00 43.63 ATOM 3193 CD LYSB 608 14.394 56.538 21.307 1.00 43.77 ATOM 3194 CE LYS B 608 13.19257.458 21.141 1.00 44.09 ATOM 3195 NZ LYS B 608 13.518 58.878 21.4571.00 43.98 ATOM 3196 C LYS B 608 13.878 52.248 21.940 1.00 26.36 ATOM3197 O LYS B 608 14.221 51.870 23.062 1.00 27.18 ATOM 3198 N ASN B 60912.606 52.277 21.559 1.00 24.76 ATOM 3199 CA ASN B 609 11.560 51.89022.490 1.00 25.81 ATOM 3200 CB ASN B 609 10.305 52.718 22.222 1.00 34.37ATOM 3201 CG ASN B 609 10.558 54.201 22.378 1.00 35.05 ATOM 3202 OD1 ASNB 609 10.969 54.657 23.444 1.00 35.79 ATOM 3203 ND2 ASN B 609 10.32654.961 21.315 1.00 35.63 ATOM 3204 C ASN B 609 11.226 50.406 22.548 1.0024.40 ATOM 3205 O ASN B 609 10.336 49.993 23.294 1.00 24.72 ATOM 3206 NVAL B 610 11.925 49.596 21.759 1.00 22.64 ATOM 3207 CA VAL B 610 11.69948.160 21.814 1.00 21.87 ATOM 3208 CB VAL B 610 12.205 47.456 20.5361.00 21.44 ATOM 3209 CG1 VAL B 610 12.237 45.953 20.746 1.00 21.17 ATOM3210 CG2 VAL B 610 11.276 47.783 19.377 1.00 21.07 ATOM 3211 C VAL B 61012.513 47.729 23.037 1.00 22.60 ATOM 3212 O VAL B 610 13.704 48.01623.127 1.00 22.78 ATOM 3213 N ALA B 611 11.865 47.051 23.976 1.00 21.43ATOM 3214 CA ALA B 611 12.500 46.651 25.232 1.00 21.58 ATOM 3215 CB ALAB 611 11.521 45.828 26.061 1.00 24.34 ATOM 3216 C ALA B 611 13.85145.941 25.176 1.00 21.37 ATOM 3217 O ALA B 611 14.795 46.361 25.851 1.0021.07 ATOM 3218 N TYR B 612 13.951 44.878 24.382 1.00 20.78 ATOM 3219 CATYR B 612 15.202 44.119 24.301 1.00 19.11 ATOM 3220 CB TYR B 612 14.92642.648 24.623 1.00 19.45 ATOM 3221 CG TYR B 612 16.144 41.756 24.4931.00 19.72 ATOM 3222 CD1 TYR B 612 16.194 40.756 23.523 1.00 19.82 ATOM3223 CE1 TYR B 612 17.304 39.933 23.401 1.00 19.95 ATOM 3224 CD2 TYR B612 17.238 41.914 25.337 1.00 19.48 ATOM 3225 CE2 TYR B 612 18.35941.094 25.222 1.00 20.02 ATOM 3226 CZ TYR B 612 18.382 40.109 24.2591.00 20.21 ATOM 3227 OH TYR B 612 19.471 39.271 24.168 1.00 20.28 ATOM3228 C TYR B 612 15.994 44.218 22.994 1.00 20.06 ATOM 3229 O TYR B 61217.203 44.465 23.027 1.00 19.27 ATOM 3230 N HIS B 613 15.338 44.02121.851 1.00 20.51 ATOM 3231 CA HIS B 613 16.046 44.096 20.569 1.00 19.40ATOM 3232 CB HIS B 613 15.310 43.290 19.493 1.00 21.37 ATOM 3233 CG HISB 613 15.351 41.811 19.712 1.00 21.97 ATOM 3234 CD2 HIS B 613 16.33840.907 19.503 1.00 21.44 ATOM 3235 ND1 HIS B 613 14.283 41.101 20.2161.00 21.50 ATOM 3236 CE1 HIS B 613 14.608 39.824 20.307 1.00 22.37 ATOM3237 NE2 HIS B 613 15.851 39.679 19.881 1.00 22.50 ATOM 3238 C HIS B 61316.229 45.530 20.093 1.00 19.18 ATOM 3239 O HIS B 613 15.583 45.97119.149 1.00 19.28 ATOM 3240 N ASN B 614 17.137 46.241 20.749 1.00 19.04ATOM 3241 CA ASN B 614 17.429 47.631 20.425 1.00 19.60 ATOM 3242 CB ASNB 614 16.895 48.526 21.541 1.00 24.32 ATOM 3243 CG ASN B 614 17.24547.996 22.914 1.00 24.73 ATOM 3244 OD1 ASN B 614 18.405 47.678 23.1881.00 26.31 ATOM 3245 ND2 ASN B 614 16.247 47.890 23.787 1.00 24.39 ATOM3246 C ASN B 614 18.948 47.761 20.311 1.00 19.61 ATOM 3247 O ASN B 61419.658 46.757 20.336 1.00 19.88 ATOM 3248 N TRP B 615 19.451 48.98620.188 1.00 20.60 ATOM 3249 CA TRP B 615 20.893 49.189 20.052 1.00 20.16ATOM 3250 CB TRP B 615 21.219 50.686 20.022 1.00 22.74 ATOM 3251 CG TRPB 615 22.672 50.982 20.262 1.00 23.84 ATOM 3252 CD2 TRP B 615 23.77350.638 19.412 1.00 23.87 ATOM 3253 CE2 TRP B 615 24.949 51.101 20.0461.00 24.13 ATOM 3254 CE3 TRP B 615 23.882 49.985 18.179 1.00 24.34 ATOM3255 CD1 TRP B 615 23.209 51.620 21.346 1.00 23.95 ATOM 3256 NE1 TRP B615 24.574 51.694 21.224 1.00 24.06 ATOM 3257 CZ2 TRP B 615 26.22250.932 19.485 1.00 24.74 ATOM 3258 CZ3 TRP B 615 25.152 49.816 17.6181.00 24.67 ATOM 3259 CH2 TRP B 615 26.304 50.290 18.276 1.00 23.93 ATOM3260 C TRP B 615 21.776 48.514 21.098 1.00 19.91 ATOM 3261 O TRP B 61522.834 47.960 20.766 1.00 18.94 ATOM 3262 N ARG B 616 21.373 48.57222.361 1.00 18.07 ATOM 3263 CA ARG B 616 22.193 47.978 23.403 1.00 19.36ATOM 3264 CB ARG B 616 21.610 48.286 24.785 1.00 22.36 ATOM 3265 CG ARGB 616 21.612 49.788 25.119 1.00 22.18 ATOM 3266 CD ARG B 616 23.02950.377 25.052 1.00 22.30 ATOM 3267 NE ARG B 616 23.086 51.816 25.3131.00 23.22 ATOM 3268 CZ ARG B 616 23.686 52.364 26.368 1.00 23.02 ATOM3269 NH1 ARG B 616 24.280 51.600 27.272 1.00 22.92 ATOM 3270 NH2 ARG B616 23.714 53.685 26.504 1.00 23.10 ATOM 3271 C ARG B 616 22.392 46.47923.208 1.00 18.33 ATOM 3272 O ARG B 616 23.483 45.970 23.476 1.00 18.59ATOM 3273 N HIS B 617 21.363 45.772 22.736 1.00 20.45 ATOM 3274 CA HIS B617 21.495 44.333 22.512 1.00 17.68 ATOM 3275 CB HIS B 617 20.156 43.69022.143 1.00 17.10 ATOM 3276 CG HIS B 617 20.300 42.309 21.571 1.00 16.72ATOM 3277 CD2 HIS B 617 20.008 41.819 20.343 1.00 19.45 ATOM 3278 ND1HIS B 617 20.842 41.261 22.283 1.00 17.70 ATOM 3279 CE1 HIS B 617 20.88040.183 21.517 1.00 16.30 ATOM 3280 NE2 HIS B 617 20.380 40.497 20.3361.00 14.56 ATOM 3281 C HIS B 617 22.507 44.058 21.402 1.00 18.17 ATOM3282 O HIS B 617 23.343 43.151 21.528 1.00 17.84 ATOM 3283 N ALA B 61822.420 44.836 20.326 1.00 18.42 ATOM 3284 CA ALA B 618 23.329 44.70719.189 1.00 17.70 ATOM 3285 CB ALA B 618 22.918 45.659 18.067 1.00 21.95ATOM 3286 C ALA B 618 24.749 45.026 19.652 1.00 17.93 ATOM 3287 O ALA B618 25.701 44.320 19.324 1.00 18.41 ATOM 3288 N PHE B 619 24.882 46.10020.421 1.00 17.19 ATOM 3289 CA PHE B 619 26.184 46.502 20.936 1.00 17.81ATOM 3290 CB PHE B 619 26.040 47.811 21.726 1.00 18.98 ATOM 3291 CG PHEB 619 27.290 48.224 22.454 1.00 18.41 ATOM 3292 CD1 PHE B 619 28.42348.626 21.755 1.00 18.73 ATOM 3293 CD2 PHE B 619 27.340 48.172 23.8421.00 19.11 ATOM 3294 CE1 PHE B 619 29.588 48.966 22.427 1.00 19.47 ATOM3295 CE2 PHE B 619 28.498 48.509 24.527 1.00 19.39 ATOM 3296 CZ PHE B619 29.627 48.907 23.816 1.00 19.32 ATOM 3297 C PHE B 619 26.791 45.40721.818 1.00 18.52 ATOM 3298 O PHE B 619 27.979 45.091 21.695 1.00 18.60ATOM 3299 N ASN B 620 25.983 44.819 22.699 1.00 18.74 ATOM 3300 CA ASN B620 26.484 43.774 23.585 1.00 19.38 ATOM 3301 CB ASN B 620 25.457 43.42424.670 1.00 22.15 ATOM 3302 CG ASN B 620 25.289 44.538 25.691 1.00 22.79ATOM 3303 OD1 ASN B 620 26.218 45.288 25.941 1.00 23.65 ATOM 3304 ND2ASN B 620 24.110 44.632 26.292 1.00 22.68 ATOM 3305 C ASN B 620 26.85742.524 22.806 1.00 18.58 ATOM 3306 O ASN B 620 27.787 41.809 23.178 1.0019.87 ATOM 3307 N THR B 621 26.134 42.262 21.723 1.00 19.05 ATOM 3308 CATHR B 621 26.438 41.099 20.903 1.00 18.12 ATOM 3309 CB THR B 621 25.35240.874 19.823 1.00 17.52 ATOM 3310 OG1 THR B 621 24.095 40.640 20.4621.00 18.11 ATOM 3311 CG2 THR B 621 25.694 39.657 18.953 1.00 18.01 ATOM3312 C THR B 621 27.796 41.323 20.233 1.00 18.57 ATOM 3313 O THR B 62128.601 40.398 20.134 1.00 19.61 ATOM 3314 N ALA B 622 28.046 42.55019.785 1.00 19.36 ATOM 3315 CA ALA B 622 29.310 42.896 19.140 1.00 18.22ATOM 3316 CB ALA B 622 29.221 44.288 18.511 1.00 22.38 ATOM 3317 C ALA B622 30.452 42.843 20.152 1.00 20.92 ATOM 3318 O ALA B 622 31.555 42.40719.829 1.00 18.90 ATOM 3319 N GLN B 623 30.192 43.285 21.381 1.00 17.97ATOM 3320 CA GLN B 623 31.219 43.257 22.420 1.00 19.34 ATOM 3321 CB GLNB 623 30.709 43.970 23.677 1.00 20.66 ATOM 3322 CG GLN B 623 31.72044.081 24.823 1.00 21.04 ATOM 3323 CD GLN B 623 31.756 42.848 25.7041.00 21.30 ATOM 3324 OE1 GLN B 623 30.712 42.346 26.134 1.00 22.15 ATOM3325 NE2 GLN B 623 32.956 42.362 25.995 1.00 21.86 ATOM 3326 C GLN B 62331.600 41.811 22.739 1.00 18.06 ATOM 3327 O GLN B 623 32.776 41.49922.963 1.00 19.37 ATOM 3328 N CYS B 624 30.609 40.924 22.755 1.00 18.07ATOM 3329 CA CYS B 624 30.880 39.519 23.027 1.00 17.94 ATOM 3330 CB CYSB 624 29.585 38.724 23.171 1.00 21.24 ATOM 3331 SG CYS B 624 29.85737.007 23.684 1.00 20.09 ATOM 3332 C CYS B 624 31.695 38.961 21.866 1.0019.06 ATOM 3333 O CYS B 624 32.615 38.158 22.067 1.00 18.98 ATOM 3334 NMET B 625 31.371 39.400 20.653 1.00 18.53 ATOM 3335 CA MET B 625 32.10238.937 19.470 1.00 18.30 ATOM 3336 CB MET B 625 31.491 39.521 18.1951.00 19.41 ATOM 3337 CG MET B 625 32.164 39.070 16.897 1.00 19.09 ATOM3338 SD MET B 625 32.084 37.274 16.604 1.00 16.39 ATOM 3339 CE MET B 62530.324 37.033 16.399 1.00 18.22 ATOM 3340 C MET B 625 33.555 39.39319.606 1.00 18.55 ATOM 3341 O MET B 625 34.483 38.640 19.332 1.00 19.67ATOM 3342 N PHE B 626 33.749 40.636 20.036 1.00 19.00 ATOM 3343 CA PHE B626 35.101 41.156 20.225 1.00 18.99 ATOM 3344 CB PHE B 626 35.063 42.62520.649 1.00 19.58 ATOM 3345 CG PHE B 626 36.421 43.211 20.909 1.00 19.51ATOM 3346 CD1 PHE B 626 36.965 43.200 22.190 1.00 21.50 ATOM 3347 CD2PHE B 626 37.162 43.759 19.868 1.00 20.23 ATOM 3348 CE1 PHE B 626 38.23443.731 22.433 1.00 19.73 ATOM 3349 CE2 PHE B 626 38.433 44.292 20.0951.00 20.70 ATOM 3350 CZ PHE B 626 38.971 44.277 21.384 1.00 20.75 ATOM3351 C PHE B 626 35.851 40.352 21.279 1.00 20.36 ATOM 3352 O PHE B 62636.993 39.951 21.066 1.00 19.87 ATOM 3353 N ALA B 627 35.211 40.11722.420 1.00 20.43 ATOM 3354 CA ALA B 627 35.853 39.367 23.490 1.00 21.24ATOM 3355 CB ALA B 627 34.950 39.322 24.713 1.00 23.11 ATOM 3356 C ALA B627 36.192 37.949 23.033 1.00 20.95 ATOM 3357 O ALA B 627 37.274 37.43323.329 1.00 21.81 ATOM 3358 N ALA B 628 35.267 37.327 22.305 1.00 19.64ATOM 3359 CA ALA B 628 35.474 35.970 21.808 1.00 18.50 ATOM 3360 CB ALAB 628 34.194 35.453 21.156 1.00 21.27 ATOM 3361 C ALA B 628 36.61935.901 20.808 1.00 18.67 ATOM 3362 O ALA B 628 37.415 34.958 20.827 1.0021.28 ATOM 3363 N LEU B 629 36.695 36.890 19.921 1.00 19.77 ATOM 3364 CALEU B 629 37.748 36.926 18.911 1.00 20.08 ATOM 3365 CB LEU B 629 37.44938.026 17.885 1.00 20.64 ATOM 3366 CG LEU B 629 36.265 37.740 16.9571.00 20.56 ATOM 3367 CD1 LEU B 629 35.933 38.980 16.138 1.00 20.95 ATOM3368 CD2 LEU B 629 36.612 36.556 16.048 1.00 21.88 ATOM 3369 C LEU B 62939.097 37.175 19.565 1.00 20.23 ATOM 3370 O LEU B 629 40.083 36.50519.254 1.00 20.58 ATOM 3371 N LYS B 630 39.131 38.142 20.478 1.00 22.49ATOM 3372 CA LYS B 630 40.354 38.517 21.184 1.00 24.06 ATOM 3373 CB LYSB 630 40.218 39.936 21.730 1.00 29.47 ATOM 3374 CG LYS B 630 40.46741.003 20.712 1.00 30.15 ATOM 3375 CD LYS B 630 41.918 40.980 20.3041.00 30.05 ATOM 3376 CE LYS B 630 42.193 42.037 19.271 1.00 29.88 ATOM3377 NZ LYS B 630 43.597 41.963 18.828 1.00 29.81 ATOM 3378 C LYS B 63040.727 37.597 22.331 1.00 24.07 ATOM 3379 O LYS B 630 41.585 36.72422.197 1.00 23.83 ATOM 3380 N ALA B 631 40.091 37.815 23.475 1.00 24.13ATOM 3381 CA ALA B 631 40.368 37.020 24.659 1.00 24.70 ATOM 3382 CB ALAB 631 39.527 37.516 25.828 1.00 25.17 ATOM 3383 C ALA B 631 40.12135.534 24.437 1.00 25.41 ATOM 3384 O ALA B 631 40.882 34.700 24.922 1.0025.73 ATOM 3385 N GLY B 632 39.060 35.203 23.705 1.00 24.21 ATOM 3386 CAGLY B 632 38.743 33.804 23.468 1.00 23.42 ATOM 3387 C GLY B 632 39.58633.166 22.380 1.00 22.70 ATOM 3388 O GLY B 632 39.440 31.978 22.090 1.0024.46 ATOM 3389 N LYS B 633 40.456 33.968 21.775 1.00 23.53 ATOM 3390 CALYS B 633 41.357 33.531 20.717 1.00 24.70 ATOM 3391 CB LYS B 633 42.41932.592 21.292 1.00 32.80 ATOM 3392 CG LYS B 633 43.316 33.272 22.3101.00 33.19 ATOM 3393 CD LYS B 633 44.524 32.424 22.662 1.00 33.59 ATOM3394 CE LYS B 633 45.416 33.167 23.643 1.00 33.78 ATOM 3395 NZ LYS B 63345.749 34.527 23.130 1.00 34.10 ATOM 3396 C LYS B 633 40.709 32.88819.499 1.00 24.23 ATOM 3397 O LYS B 633 41.243 31.935 18.928 1.00 24.88ATOM 3398 N ILE B 634 39.565 33.411 19.079 1.00 22.51 ATOM 3399 CA ILE B634 38.911 32.861 17.907 1.00 20.76 ATOM 3400 CB ILE B 634 37.376 32.98218.036 1.00 22.93 ATOM 3401 CG2 ILE B 634 36.694 32.531 16.750 1.0023.15 ATOM 3402 CG1 ILE B 634 36.907 32.122 19.218 1.00 22.60 ATOM 3403CD1 ILE B 634 35.410 32.116 19.444 1.00 24.49 ATOM 3404 C ILE B 63439.424 33.612 16.680 1.00 21.02 ATOM 3405 O ILE B 634 39.394 33.10915.559 1.00 21.18 ATOM 3406 N GLN B 635 39.920 34.821 16.911 1.00 20.73ATOM 3407 CA GLN B 635 40.453 35.656 15.848 1.00 21.87 ATOM 3408 CB GLNB 635 41.023 36.933 16.464 1.00 28.05 ATOM 3409 CG GLN B 635 41.70337.868 15.503 1.00 29.39 ATOM 3410 CD GLN B 635 42.362 39.034 16.2171.00 27.87 ATOM 3411 OE1 GLN B 635 43.020 39.856 15.596 1.00 29.76 ATOM3412 NE2 GLN B 635 42.178 39.110 17.532 1.00 27.16 ATOM 3413 C GLN B 63541.543 34.904 15.089 1.00 22.14 ATOM 3414 O GLN B 635 41.600 34.93413.858 1.00 21.83 ATOM 3415 N ASN B 636 42.387 34.224 15.854 1.00 23.53ATOM 3416 CA ASN B 636 43.504 33.447 15.335 1.00 24.32 ATOM 3417 CB ASNB 636 44.216 32.735 16.486 1.00 22.54 ATOM 3418 CG ASN B 636 44.60733.675 17.606 1.00 22.42 ATOM 3419 OD1 ASN B 636 45.788 33.821 17.9211.00 23.23 ATOM 3420 ND2 ASN B 636 43.620 34.307 18.221 1.00 21.19 ATOM3421 C ASN B 636 43.089 32.390 14.325 1.00 24.28 ATOM 3422 O ASN B 63643.868 32.022 13.443 1.00 24.97 ATOM 3423 N LYS B 637 41.864 31.89914.463 1.00 22.71 ATOM 3424 CA LYS B 637 41.355 30.842 13.597 1.00 22.76ATOM 3425 CB LYS B 637 40.417 29.948 14.409 1.00 25.00 ATOM 3426 CG LYSB 637 41.028 29.410 15.688 1.00 25.88 ATOM 3427 CD LYS B 637 39.98328.674 16.515 1.00 24.87 ATOM 3428 CE LYS B 637 40.570 28.186 17.8201.00 26.38 ATOM 3429 NZ LYS B 637 41.716 27.261 17.598 1.00 26.67 ATOM3430 C LYS B 637 40.630 31.305 12.341 1.00 22.83 ATOM 3431 O LYS B 63740.289 30.488 11.483 1.00 22.28 ATOM 3432 N LEU B 638 40.407 32.61012.218 1.00 21.88 ATOM 3433 CA LEU B 638 39.669 33.131 11.081 1.00 22.21ATOM 3434 CB LEU B 638 38.421 33.855 11.601 1.00 18.60 ATOM 3435 CG LEUB 638 37.598 33.093 12.650 1.00 20.22 ATOM 3436 CD1 LEU B 638 36.50734.001 13.212 1.00 18.99 ATOM 3437 CD2 LEU B 638 36.985 31.847 12.0351.00 19.54 ATOM 3438 C LEU B 638 40.447 34.061 10.160 1.00 21.99 ATOM3439 O LEU B 638 41.531 34.549 10.502 1.00 21.62 ATOM 3440 N THR B 63939.878 34.299 8.982 1.00 19.43 ATOM 3441 CA THR B 639 40.474 35.1887.998 1.00 20.58 ATOM 3442 CB THR B 639 39.900 34.937 6.593 1.00 24.74ATOM 3443 OG1 THR B 639 38.501 35.257 6.581 1.00 23.76 ATOM 3444 CG2 THRB 639 40.075 33.472 6.195 1.00 24.89 ATOM 3445 C THR B 639 40.110 36.6098.413 1.00 20.43 ATOM 3446 O THR B 639 39.185 36.802 9.203 1.00 20.14ATOM 3447 N ASP B 640 40.828 37.594 7.884 1.00 22.11 ATOM 3448 CA ASP B640 40.550 38.989 8.195 1.00 21.37 ATOM 3449 CB ASP B 640 41.576 39.9087.528 1.00 24.51 ATOM 3450 CG ASP B 640 42.964 39.763 8.119 1.00 24.64ATOM 3451 OD1 ASP B 640 43.900 40.381 7.575 1.00 23.86 ATOM 3452 OD2 ASPB 640 43.118 39.040 9.124 1.00 24.36 ATOM 3453 C ASP B 640 39.150 39.3607.718 1.00 22.46 ATOM 3454 O ASP B 640 38.440 40.094 8.398 1.00 21.08ATOM 3455 N LEU B 641 38.761 38.850 6.549 1.00 22.62 ATOM 3456 CA LEU B641 37.436 39.127 5.988 1.00 22.81 ATOM 3457 CB LEU B 641 37.312 38.5044.594 1.00 24.97 ATOM 3458 CG LEU B 641 37.449 39.409 3.365 1.00 27.28ATOM 3459 CD1 LEU B 641 38.476 40.500 3.601 1.00 25.76 ATOM 3460 CD2 LEUB 641 37.793 38.557 2.152 1.00 25.23 ATOM 3461 C LEU B 641 36.338 38.5746.888 1.00 22.25 ATOM 3462 O LEU B 641 35.295 39.204 7.086 1.00 21.31ATOM 3463 N GLU B 642 36.561 37.379 7.417 1.00 20.49 ATOM 3464 CA GLU B642 35.588 36.765 8.301 1.00 20.51 ATOM 3465 CB GLU B 642 36.005 35.3278.615 1.00 24.37 ATOM 3466 CG GLU B 642 35.704 34.391 7.460 1.00 24.67ATOM 3467 CD GLU B 642 36.405 33.053 7.574 1.00 24.64 ATOM 3468 OE1 GLUB 642 36.092 32.159 6.760 1.00 27.01 ATOM 3469 OE2 GLU B 642 37.26732.893 8.461 1.00 24.86 ATOM 3470 C GLU B 642 35.427 37.579 9.581 1.0020.92 ATOM 3471 O GLU B 642 34.309 37.764 10.069 1.00 20.75 ATOM 3472 NILE B 643 36.542 38.076 10.108 1.00 21.11 ATOM 3473 CA ILE B 643 36.52938.880 11.325 1.00 19.45 ATOM 3474 CB ILE B 643 37.973 39.195 11.7711.00 22.34 ATOM 3475 CG2 ILE B 643 37.970 40.210 12.912 1.00 21.69 ATOM3476 CG1 ILE B 643 38.652 37.895 12.217 1.00 20.78 ATOM 3477 CD1 ILE B643 40.165 37.993 12.357 1.00 22.35 ATOM 3478 C ILE B 643 35.762 40.17711.055 1.00 19.94 ATOM 3479 O ILE B 643 34.921 40.598 11.858 1.00 19.49ATOM 3480 N LEU B 644 36.044 40.790 9.911 1.00 19.97 ATOM 3481 CA LEU B644 35.385 42.027 9.502 1.00 19.99 ATOM 3482 CB LEU B 644 35.926 42.4668.135 1.00 21.41 ATOM 3483 CG LEU B 644 35.277 43.650 7.415 1.00 21.06ATOM 3484 CD1 LEU B 644 35.449 44.915 8.234 1.00 22.38 ATOM 3485 CD2 LEUB 644 35.921 43.809 6.042 1.00 21.65 ATOM 3486 C LEU B 644 33.877 41.8179.409 1.00 21.45 ATOM 3487 O LEU B 644 33.093 42.583 9.970 1.00 18.41ATOM 3488 N ALA B 645 33.485 40.770 8.691 1.00 19.49 ATOM 3489 CA ALA B645 32.076 40.444 8.499 1.00 20.21 ATOM 3490 CB ALA B 645 31.940 39.2667.539 1.00 18.61 ATOM 3491 C ALA B 645 31.371 40.125 9.806 1.00 20.78ATOM 3492 O ALA B 645 30.229 40.535 10.009 1.00 19.80 ATOM 3493 N LEU B646 32.047 39.395 10.688 1.00 17.92 ATOM 3494 CA LEU B 646 31.455 39.02811.968 1.00 18.51 ATOM 3495 CB LEU B 646 32.381 38.084 12.735 1.00 21.14ATOM 3496 CG LEU B 646 32.393 36.631 12.250 1.00 19.75 ATOM 3497 CD1 LEUB 646 33.560 35.903 12.894 1.00 20.35 ATOM 3498 CD2 LEU B 646 31.07735.951 12.587 1.00 20.12 ATOM 3499 C LEU B 646 31.138 40.241 12.837 1.0017.72 ATOM 3500 O LEU B 646 30.075 40.304 13.460 1.00 18.91 ATOM 3501 NLEU B 647 32.054 41.202 12.893 1.00 18.38 ATOM 3502 CA LEU B 647 31.81542.387 13.710 1.00 18.99 ATOM 3503 CB LEU B 647 33.074 43.255 13.8001.00 16.80 ATOM 3504 CG LEU B 647 32.940 44.461 14.734 1.00 18.47 ATOM3505 CD1 LEU B 647 32.637 43.978 16.146 1.00 18.48 ATOM 3506 CD2 LEU B647 34.221 45.278 14.707 1.00 18.50 ATOM 3507 C LEU B 647 30.666 43.20113.128 1.00 18.90 ATOM 3508 O LEU B 647 29.776 43.646 13.861 1.00 18.98ATOM 3509 N ILE B 648 30.689 43.399 11.813 1.00 18.80 ATOM 3510 CA ILE B648 29.633 44.146 11.134 1.00 17.53 ATOM 3511 CB ILE B 648 29.948 44.2989.620 1.00 17.43 ATOM 3512 CG2 ILE B 648 28.747 44.886 8.884 1.00 16.56ATOM 3513 CG1 ILE B 648 31.189 45.181 9.439 1.00 16.47 ATOM 3514 CD1 ILEB 648 31.622 45.377 7.987 1.00 16.64 ATOM 3515 C ILE B 648 28.303 43.40511.322 1.00 19.67 ATOM 3516 O ILE B 648 27.268 44.020 11.608 1.00 19.92ATOM 3517 N ALA B 649 28.327 42.084 11.170 1.00 17.14 ATOM 3518 CA ALA B649 27.105 41.297 11.335 1.00 19.06 ATOM 3519 CB ALA B 649 27.353 39.83010.964 1.00 15.65 ATOM 3520 C ALA B 649 26.562 41.381 12.753 1.00 17.80ATOM 3521 O ALA B 649 25.360 41.559 12.957 1.00 16.89 ATOM 3522 N ALA B650 27.442 41.245 13.738 1.00 17.06 ATOM 3523 CA ALA B 650 27.016 41.31615.128 1.00 16.09 ATOM 3524 CB ALA B 650 28.219 41.166 16.056 1.00 20.12ATOM 3525 C ALA B 650 26.299 42.641 15.406 1.00 17.22 ATOM 3526 O ALA B650 25.239 42.660 16.031 1.00 18.13 ATOM 3527 N LEU B 651 26.875 43.73914.935 1.00 18.31 ATOM 3528 CA LEU B 651 26.295 45.065 15.145 1.00 18.19ATOM 3529 CB LEU B 651 27.302 46.143 14.744 1.00 17.38 ATOM 3530 CG LEUB 651 28.532 46.318 15.633 1.00 17.82 ATOM 3531 CD1 LEU B 651 29.58047.146 14.917 1.00 17.72 ATOM 3532 CD2 LEU B 651 28.108 46.993 16.9391.00 16.75 ATOM 3533 C LEU B 651 25.010 45.305 14.363 1.00 19.12 ATOM3534 O LEU B 651 24.145 46.073 14.792 1.00 19.03 ATOM 3535 N SER B 65224.879 44.644 13.218 1.00 16.50 ATOM 3536 CA SER B 652 23.717 44.86112.361 1.00 15.50 ATOM 3537 CB SER B 652 24.165 45.025 10.902 1.00 19.61ATOM 3538 OG SER B 652 25.258 45.908 10.760 1.00 18.90 ATOM 3539 C SER B652 22.667 43.764 12.374 1.00 17.20 ATOM 3540 O SER B 652 21.616 43.93211.770 1.00 16.98 ATOM 3541 N HIS B 653 22.922 42.664 13.073 1.00 19.06ATOM 3542 CA HIS B 653 22.001 41.533 12.998 1.00 19.69 ATOM 3543 CB HISB 653 22.594 40.312 13.697 1.00 17.94 ATOM 3544 CG HIS B 653 22.33240.270 15.165 1.00 17.54 ATOM 3545 CD2 HIS B 653 21.396 39.612 15.8881.00 16.38 ATOM 3546 ND1 HIS B 653 23.064 41.010 16.066 1.00 17.02 ATOM3547 CE1 HIS B 653 22.592 40.809 17.282 1.00 14.84 ATOM 3548 NE2 HIS B653 21.582 39.965 17.202 1.00 19.75 ATOM 3549 C HIS B 653 20.548 41.68913.430 1.00 20.16 ATOM 3550 O HIS B 653 19.734 40.833 13.106 1.00 18.45ATOM 3551 N ASP B 654 20.206 42.762 14.143 1.00 15.51 ATOM 3552 CA ASP B654 18.808 42.945 14.562 1.00 15.82 ATOM 3553 CB ASP B 654 18.680 42.84816.082 1.00 17.70 ATOM 3554 CG ASP B 654 18.401 41.444 16.565 1.00 16.46ATOM 3555 OD1 ASP B 654 17.724 40.681 15.845 1.00 17.13 ATOM 3556 OD2ASP B 654 18.826 41.109 17.689 1.00 16.53 ATOM 3557 C ASP B 654 18.24644.300 14.120 1.00 15.98 ATOM 3558 O ASP B 654 17.249 44.775 14.679 1.0016.02 ATOM 3559 N LEU B 655 18.875 44.903 13.113 1.00 14.12 ATOM 3560 CALEU B 655 18.474 46.212 12.585 1.00 16.45 ATOM 3561 CB LEU B 655 19.19146.465 11.253 1.00 22.99 ATOM 3562 CG LEU B 655 20.250 47.557 11.0431.00 25.93 ATOM 3563 CD1 LEU B 655 20.660 48.211 12.341 1.00 24.18 ATOM3564 CD2 LEU B 655 21.435 46.946 10.315 1.00 23.72 ATOM 3565 C LEU B 65516.968 46.355 12.374 1.00 15.99 ATOM 3566 O LEU B 655 16.332 45.48811.777 1.00 16.81 ATOM 3567 N ASP B 656 16.403 47.452 12.877 1.00 18.46ATOM 3568 CA ASP B 656 14.975 47.741 12.723 1.00 18.67 ATOM 3569 CB ASPB 656 14.676 48.025 11.243 1.00 19.71 ATOM 3570 CG ASP B 656 13.31848.677 11.028 1.00 21.79 ATOM 3571 OD1 ASP B 656 12.968 49.591 11.8031.00 19.47 ATOM 3572 OD2 ASP B 656 12.612 48.282 10.075 1.00 21.77 ATOM3573 C ASP B 656 14.046 46.647 13.244 1.00 19.00 ATOM 3574 O ASP B 65612.965 46.434 12.697 1.00 18.21 ATOM 3575 N HIS B 657 14.460 45.95214.298 1.00 17.23 ATOM 3576 CA HIS B 657 13.631 44.899 14.864 1.00 16.33ATOM 3577 CB HIS B 657 14.377 44.174 15.983 1.00 19.47 ATOM 3578 CG HISB 657 13.705 42.915 16.419 1.00 18.64 ATOM 3579 CD2 HIS B 657 12.47542.701 16.941 1.00 17.65 ATOM 3580 ND1 HIS B 657 14.300 41.673 16.3181.00 19.33 ATOM 3581 CE1 HIS B 657 13.467 40.752 16.763 1.00 16.32 ATOM3582 NE2 HIS B 657 12.352 41.349 17.147 1.00 20.76 ATOM 3583 C HIS B 65712.352 45.546 15.409 1.00 17.90 ATOM 3584 O HIS B 657 12.419 46.52916.151 1.00 17.75 ATOM 3585 N PRO B 658 11.176 45.011 15.034 1.00 19.30ATOM 3586 CD PRO B 658 11.026 43.936 14.032 1.00 15.12 ATOM 3587 CA PROB 658 9.863 45.519 15.463 1.00 20.23 ATOM 3588 CB PRO B 658 8.922 44.97014.398 1.00 15.90 ATOM 3589 CG PRO B 658 9.539 43.612 14.093 1.00 14.22ATOM 3590 C PRO B 658 9.422 45.146 16.877 1.00 19.73 ATOM 3591 O PRO B658 8.411 45.650 17.371 1.00 20.21 ATOM 3592 N GLY B 659 10.160 44.25817.530 1.00 20.02 ATOM 3593 CA GLY B 659 9.800 43.886 18.884 1.00 20.59ATOM 3594 C GLY B 659 8.794 42.760 18.918 1.00 20.21 ATOM 3595 O GLY B659 8.194 42.491 19.954 1.00 21.72 ATOM 3596 N VAL B 660 8.589 42.11717.772 1.00 20.05 ATOM 3597 CA VAL B 660 7.685 40.980 17.675 1.00 19.03ATOM 3598 CB VAL B 660 6.353 41.336 16.963 1.00 22.30 ATOM 3599 CG1 VALB 660 5.551 42.293 17.825 1.00 23.15 ATOM 3600 CG2 VAL B 660 6.62341.946 15.599 1.00 22.17 ATOM 3601 C VAL B 660 8.432 39.915 16.882 1.0020.57 ATOM 3602 O VAL B 660 9.340 40.233 16.115 1.00 20.96 ATOM 3603 NSER B 661 8.043 38.660 17.068 1.00 18.27 ATOM 3604 CA SER B 661 8.70737.525 16.413 1.00 19.30 ATOM 3605 CB SER B 661 8.450 36.256 17.217 1.0023.22 ATOM 3606 OG SER B 661 7.108 35.823 17.058 1.00 22.03 ATOM 3607 CSER B 661 8.337 37.237 14.961 1.00 19.20 ATOM 3608 O SER B 661 7.41037.814 14.402 1.00 16.38 ATOM 3609 N ASN B 662 9.080 36.311 14.360 1.0018.48 ATOM 3610 CA ASN B 662 8.810 35.905 12.989 1.00 17.98 ATOM 3611 CBASN B 662 9.832 34.868 12.521 1.00 19.15 ATOM 3612 CG ASN B 662 11.11735.491 12.060 1.00 20.55 ATOM 3613 OD1 ASN B 662 11.113 36.584 11.5041.00 18.07 ATOM 3614 ND2 ASN B 662 12.229 34.788 12.263 1.00 19.60 ATOM3615 C ASN B 662 7.428 35.275 12.943 1.00 18.27 ATOM 3616 O ASN B 6626.651 35.512 12.020 1.00 19.29 ATOM 3617 N GLN B 663 7.129 34.463 13.9521.00 19.10 ATOM 3618 CA GLN B 663 5.845 33.793 14.020 1.00 19.98 ATOM3619 CB GLN B 663 5.763 32.909 15.267 1.00 47.82 ATOM 3620 CG GLN B 6636.544 31.609 15.160 1.00 48.95 ATOM 3621 CD GLN B 663 8.056 31.79315.228 1.00 49.43 ATOM 3622 OE1 GLN B 663 8.814 30.853 14.978 1.00 49.36ATOM 3623 NE2 GLN B 663 8.499 32.997 15.576 1.00 48.96 ATOM 3624 C GLN B663 4.708 34.798 14.029 1.00 19.45 ATOM 3625 O GLN B 663 3.701 34.60913.352 1.00 19.22 ATOM 3626 N PHE B 664 4.883 35.869 14.795 1.00 17.76ATOM 3627 CA PHE B 664 3.866 36.909 14.888 1.00 18.71 ATOM 3628 CB PHE B664 4.266 37.946 15.938 1.00 20.58 ATOM 3629 CG PHE B 664 3.280 39.07716.084 1.00 20.67 ATOM 3630 CD1 PHE B 664 3.340 40.185 15.243 1.00 20.97ATOM 3631 CD2 PHE B 664 2.291 39.031 17.064 1.00 20.35 ATOM 3632 CE1 PHEB 664 2.428 41.232 15.377 1.00 20.58 ATOM 3633 CE2 PHE B 664 1.37740.074 17.203 1.00 21.94 ATOM 3634 CZ PHE B 664 1.448 41.174 16.357 1.0021.03 ATOM 3635 C PHE B 664 3.691 37.571 13.525 1.00 17.64 ATOM 3636 OPHE B 664 2.574 37.781 13.071 1.00 17.39 ATOM 3637 N LEU B 665 4.80137.883 12.865 1.00 18.84 ATOM 3638 CA LEU B 665 4.734 38.504 11.552 1.0020.08 ATOM 3639 CB LEU B 665 6.146 38.866 11.078 1.00 18.16 ATOM 3640 CGLEU B 665 6.834 39.975 11.886 1.00 19.07 ATOM 3641 CD1 LEU B 665 8.28840.092 11.490 1.00 19.47 ATOM 3642 CD2 LEU B 665 6.119 41.289 11.6541.00 18.80 ATOM 3643 C LEU B 665 4.039 37.582 10.540 1.00 20.00 ATOM3644 O LEU B 665 3.350 38.044 9.627 1.00 21.88 ATOM 3645 N ILE B 6664.222 36.276 10.700 1.00 18.71 ATOM 3646 CA ILE B 666 3.593 35.317 9.8061.00 19.12 ATOM 3647 CB ILE B 666 4.239 33.920 9.951 1.00 22.08 ATOM3648 CG2 ILE B 666 3.423 32.879 9.199 1.00 21.74 ATOM 3649 CG1 ILE B 6665.674 33.967 9.421 1.00 21.76 ATOM 3650 CD1 ILE B 666 6.456 32.684 9.6191.00 21.29 ATOM 3651 C ILE B 666 2.104 35.218 10.119 1.00 18.58 ATOM3652 O ILE B 666 1.274 35.193 9.211 1.00 20.21 ATOM 3653 N ASN B 6671.773 35.183 11.408 1.00 21.92 ATOM 3654 CA ASN B 667 0.378 35.07211.837 1.00 22.79 ATOM 3655 CB ASN B 667 0.295 34.756 13.334 1.00 23.85ATOM 3656 CG ASN B 667 0.779 33.354 13.669 1.00 23.91 ATOM 3657 OD1 ASNB 667 0.712 32.444 12.843 1.00 24.94 ATOM 3658 ND2 ASN B 667 1.25033.173 14.895 1.00 23.83 ATOM 3659 C ASN B 667 −0.472 36.305 11.544 1.0023.14 ATOM 3660 O ASN B 667 −1.702 36.213 11.470 1.00 22.85 ATOM 3661 NTHR B 668 0.169 37.459 11.392 1.00 24.81 ATOM 3662 CA THR B 668 −0.56638.677 11.086 1.00 25.96 ATOM 3663 CB THR B 668 −0.019 39.894 11.8821.00 21.17 ATOM 3664 OG1 THR B 668 1.404 39.984 11.714 1.00 23.05 ATOM3665 CG2 THR B 668 −0.338 39.753 13.362 1.00 22.09 ATOM 3666 C THR B 668−0.511 38.973 9.585 1.00 26.69 ATOM 3667 O THR B 668 −0.961 40.022 9.1391.00 27.70 ATOM 3668 N ASN B 669 0.026 38.030 8.815 1.00 26.73 ATOM 3669CA ASN B 669 0.138 38.169 7.362 1.00 27.16 ATOM 3670 CB ASN B 669 −1.25538.135 6.726 1.00 36.60 ATOM 3671 CG ASN B 669 −1.940 36.796 6.906 1.0036.71 ATOM 3672 OD1 ASN B 669 −1.482 35.775 6.387 1.00 36.69 ATOM 3673ND2 ASN B 669 −3.039 36.789 7.650 1.00 37.50 ATOM 3674 C ASN B 669 0.86739.453 6.978 1.00 27.24 ATOM 3675 O ASN B 669 0.440 40.195 6.088 1.0026.93 ATOM 3676 N SER B 670 1.981 39.696 7.659 1.00 23.11 ATOM 3677 CASER B 670 2.802 40.876 7.435 1.00 22.67 ATOM 3678 CB SER B 670 3.94940.898 8.448 1.00 34.05 ATOM 3679 OG SER B 670 4.874 41.925 8.154 1.0035.41 ATOM 3680 C SER B 670 3.382 40.916 6.028 1.00 22.16 ATOM 3681 OSER B 670 3.580 39.880 5.388 1.00 22.16 ATOM 3682 N GLU B 671 3.66242.125 5.548 1.00 21.76 ATOM 3683 CA GLU B 671 4.236 42.279 4.225 1.0021.00 ATOM 3684 CB GLU B 671 4.388 43.757 3.872 1.00 26.81 ATOM 3685 CGGLU B 671 4.799 43.990 2.433 1.00 26.53 ATOM 3686 CD GLU B 671 4.96345.461 2.099 1.00 27.67 ATOM 3687 OE1 GLU B 671 6.052 46.018 2.361 1.0028.24 ATOM 3688 OE2 GLU B 671 3.995 46.062 1.584 1.00 26.44 ATOM 3689 CGLU B 671 5.607 41.617 4.228 1.00 20.25 ATOM 3690 O GLU B 671 5.99640.962 3.271 1.00 20.37 ATOM 3691 N LEU B 672 6.332 41.799 5.323 1.0020.82 ATOM 3692 CA LEU B 672 7.664 41.222 5.476 1.00 21.28 ATOM 3693 CBLEU B 672 8.189 41.544 6.872 1.00 29.67 ATOM 3694 CG LEU B 672 9.52242.279 7.026 1.00 30.73 ATOM 3695 CD1 LEU B 672 9.670 43.391 6.003 1.0030.03 ATOM 3696 CD2 LEU B 672 9.588 42.833 8.438 1.00 30.18 ATOM 3697 CLEU B 672 7.610 39.711 5.277 1.00 21.18 ATOM 3698 O LEU B 672 8.47039.121 4.620 1.00 20.85 ATOM 3699 N ALA B 673 6.585 39.084 5.844 1.0021.74 ATOM 3700 CA ALA B 673 6.435 37.635 5.726 1.00 21.93 ATOM 3701 CBALA B 673 5.285 37.150 6.607 1.00 19.72 ATOM 3702 C ALA B 673 6.20237.211 4.282 1.00 22.57 ATOM 3703 O ALA B 673 6.723 36.189 3.839 1.0021.41 ATOM 3704 N LEU B 674 5.410 37.987 3.548 1.00 20.77 ATOM 3705 CALEU B 674 5.151 37.664 2.153 1.00 21.89 ATOM 3706 CB LEU B 674 4.07838.586 1.572 1.00 30.80 ATOM 3707 CG LEU B 674 3.816 38.413 0.069 1.0031.55 ATOM 3708 CD1 LEU B 674 3.312 37.005 −0.217 1.00 31.01 ATOM 3709CD2 LEU B 674 2.799 39.449 −0.391 1.00 30.99 ATOM 3710 C LEU B 674 6.43137.811 1.336 1.00 22.16 ATOM 3711 O LEU B 674 6.775 36.929 0.552 1.0021.85 ATOM 3712 N MET B 675 7.132 38.922 1.536 1.00 23.84 ATOM 3713 CAMET B 675 8.366 39.192 0.809 1.00 25.40 ATOM 3714 CB MET B 675 8.97940.513 1.278 1.00 42.14 ATOM 3715 CG MET B 675 8.153 41.746 0.946 1.0042.93 ATOM 3716 SD MET B 675 8.869 43.254 1.635 1.00 43.64 ATOM 3717 CEMET B 675 10.093 43.646 0.397 1.00 43.26 ATOM 3718 C MET B 675 9.39738.080 0.973 1.00 24.69 ATOM 3719 O MET B 675 10.072 37.706 0.010 1.0025.28 ATOM 3720 N TYR B 676 9.514 37.546 2.186 1.00 22.91 ATOM 3721 CATYR B 676 10.503 36.506 2.449 1.00 23.58 ATOM 3722 CB TYR B 676 11.31636.899 3.687 1.00 22.54 ATOM 3723 CG TYR B 676 11.987 38.248 3.527 1.0023.06 ATOM 3724 CD1 TYR B 676 11.763 39.276 4.437 1.00 23.12 ATOM 3725CE1 TYR B 676 12.338 40.539 4.259 1.00 22.13 ATOM 3726 CD2 TYR B 67612.814 38.508 2.432 1.00 24.18 ATOM 3727 CE2 TYR B 676 13.400 39.7622.247 1.00 22.56 ATOM 3728 CZ TYR B 676 13.155 40.772 3.161 1.00 23.95ATOM 3729 OH TYR B 676 13.719 42.015 2.974 1.00 23.51 ATOM 3730 C TYR B676 9.973 35.074 2.578 1.00 22.94 ATOM 3731 O TYR B 676 10.640 34.2043.144 1.00 23.18 ATOM 3732 N ASN B 677 8.781 34.840 2.034 1.00 23.86ATOM 3733 CA ASN B 677 8.137 33.524 2.034 1.00 25.01 ATOM 3734 CB ASN B677 8.760 32.633 0.948 1.00 56.05 ATOM 3735 CG ASN B 677 10.243 32.3811.169 1.00 57.14 ATOM 3736 OD1 ASN B 677 10.642 31.796 2.177 1.00 57.41ATOM 3737 ND2 ASN B 677 11.069 32.819 0.222 1.00 57.47 ATOM 3738 C ASN B677 8.139 32.783 3.373 1.00 24.18 ATOM 3739 O ASN B 677 8.385 31.5753.430 1.00 22.27 ATOM 3740 N ASP B 678 7.850 33.519 4.442 1.00 20.57ATOM 3741 CA ASP B 678 7.783 32.970 5.794 1.00 20.56 ATOM 3742 CB ASP B678 6.692 31.895 5.876 1.00 24.90 ATOM 3743 CG ASP B 678 5.310 32.4425.609 1.00 26.44 ATOM 3744 OD1 ASP B 678 5.139 33.676 5.661 1.00 24.56ATOM 3745 OD2 ASP B 678 4.386 31.632 5.359 1.00 26.91 ATOM 3746 C ASP B678 9.074 32.390 6.358 1.00 19.72 ATOM 3747 O ASP B 678 9.067 31.8437.464 1.00 21.82 ATOM 3748 N GLU B 679 10.175 32.513 5.625 1.00 18.31ATOM 3749 CA GLU B 679 11.452 31.964 6.086 1.00 18.54 ATOM 3750 CB GLU B679 12.148 31.211 4.955 1.00 42.65 ATOM 3751 CG GLU B 679 11.459 29.9424.518 1.00 43.73 ATOM 3752 CD GLU B 679 12.276 29.188 3.492 1.00 44.02ATOM 3753 OE1 GLU B 679 12.480 29.723 2.381 1.00 44.05 ATOM 3754 OE2 GLUB 679 12.723 28.066 3.803 1.00 44.29 ATOM 3755 C GLU B 679 12.407 33.0216.611 1.00 18.73 ATOM 3756 O GLU B 679 12.768 33.939 5.875 1.00 19.73ATOM 3757 N SER B 680 12.832 32.866 7.867 1.00 18.88 ATOM 3758 CA SER B680 13.758 33.798 8.506 1.00 16.49 ATOM 3759 CB SER B 680 15.197 33.5088.065 1.00 21.45 ATOM 3760 OG SER B 680 15.556 32.162 8.358 1.00 20.83ATOM 3761 C SER B 680 13.383 35.226 8.127 1.00 16.21 ATOM 3762 O SER B680 14.232 36.019 7.722 1.00 14.77 ATOM 3763 N VAL B 681 12.099 35.5368.272 1.00 17.92 ATOM 3764 CA VAL B 681 11.558 36.838 7.904 1.00 16.01ATOM 3765 CB VAL B 681 10.084 36.928 8.328 1.00 18.23 ATOM 3766 CG1 VALB 681 9.501 38.295 7.956 1.00 18.53 ATOM 3767 CG2 VAL B 681 9.295 35.8227.634 1.00 19.77 ATOM 3768 C VAL B 681 12.328 38.038 8.440 1.00 15.81ATOM 3769 O VAL B 681 12.799 38.872 7.667 1.00 17.42 ATOM 3770 N LEU B681A 12.449 38.120 9.761 1.00 15.91 ATOM 3771 CA LEU B 681A 13.16439.216 10.410 1.00 17.15 ATOM 3772 CB LEU B 681A 13.094 39.055 11.9251.00 20.96 ATOM 3773 CG LEU B 681A 11.729 39.310 12.559 1.00 24.02 ATOM3774 CD1 LEU B 681A 11.671 38.670 13.947 1.00 23.49 ATOM 3775 CD2 LEU B681A 11.500 40.805 12.619 1.00 23.37 ATOM 3776 C LEU B 681A 14.62639.293 9.997 1.00 17.72 ATOM 3777 O LEU B 681A 15.151 40.367 9.733 1.0016.37 ATOM 3778 N GLU B 682 15.281 38.141 9.936 1.00 16.35 ATOM 3779 CAGLU B 682 16.690 38.112 9.582 1.00 16.54 ATOM 3780 CB GLU B 682 17.22636.693 9.797 1.00 17.48 ATOM 3781 CG GLU B 682 17.172 36.219 11.264 1.0019.45 ATOM 3782 CD GLU B 682 15.765 35.939 11.783 1.00 17.96 ATOM 3783OE1 GLU B 682 14.873 35.587 10.975 1.00 16.02 ATOM 3784 OE2 GLU B 68215.553 36.043 13.015 1.00 18.67 ATOM 3785 C GLU B 682 16.957 38.6168.162 1.00 16.65 ATOM 3786 O GLU B 682 17.956 39.307 7.908 1.00 17.06ATOM 3787 N HIS B 683 16.068 38.286 7.233 1.00 16.83 ATOM 3788 CA HIS B683 16.225 38.780 5.880 1.00 17.12 ATOM 3789 CB HIS B 683 15.193 38.1444.953 1.00 21.77 ATOM 3790 CG HIS B 683 15.579 36.779 4.481 1.00 20.98ATOM 3791 CD2 HIS B 683 15.140 35.552 4.845 1.00 21.60 ATOM 3792 ND1 HISB 683 16.550 36.571 3.524 1.00 21.61 ATOM 3793 CE1 HIS B 683 16.69035.274 3.317 1.00 20.39 ATOM 3794 NE2 HIS B 683 15.847 34.634 4.107 1.0021.29 ATOM 3795 C HIS B 683 16.050 40.291 5.923 1.00 16.91 ATOM 3796 OHIS B 683 16.745 41.017 5.220 1.00 18.17 ATOM 3797 N HIS B 684 15.13640.756 6.772 1.00 16.37 ATOM 3798 CA HIS B 684 14.900 42.194 6.906 1.0018.67 ATOM 3799 CB HIS B 684 13.674 42.472 7.789 1.00 18.26 ATOM 3800 CGHIS B 684 13.376 43.934 7.962 1.00 19.15 ATOM 3801 CD2 HIS B 684 13.32744.714 9.068 1.00 20.53 ATOM 3802 ND1 HIS B 684 13.124 44.769 6.896 1.0020.23 ATOM 3803 CE1 HIS B 684 12.939 46.002 7.336 1.00 19.60 ATOM 3804NE2 HIS B 684 13.056 45.996 8.650 1.00 19.94 ATOM 3805 C HIS B 68416.131 42.858 7.516 1.00 18.24 ATOM 3806 O HIS B 684 16.556 43.927 7.0661.00 19.27 ATOM 3807 N HIS B 685 16.706 42.228 8.537 1.00 18.19 ATOM3808 CA HIS B 685 17.890 42.797 9.180 1.00 17.28 ATOM 3809 CB HIS B 68518.349 41.957 10.376 1.00 17.43 ATOM 3810 CG HIS B 685 17.301 41.75111.425 1.00 18.40 ATOM 3811 CD2 HIS B 685 16.971 40.654 12.148 1.0018.57 ATOM 3812 ND1 HIS B 685 16.479 42.765 11.871 1.00 17.46 ATOM 3813CE1 HIS B 685 15.689 42.299 12.823 1.00 17.20 ATOM 3814 NE2 HIS B 68515.967 41.022 13.011 1.00 17.24 ATOM 3815 C HIS B 685 19.028 42.9088.175 1.00 18.93 ATOM 3816 O HIS B 685 19.725 43.919 8.140 1.00 16.49ATOM 3817 N PHE B 686 19.227 41.870 7.363 1.00 18.43 ATOM 3818 CA PHE B686 20.289 41.922 6.363 1.00 19.77 ATOM 3819 CB PHE B 686 20.430 40.5875.625 1.00 22.01 ATOM 3820 CG PHE B 686 21.424 40.635 4.501 1.00 22.74ATOM 3821 CD1 PHE B 686 22.771 40.879 4.757 1.00 22.40 ATOM 3822 CD2 PHEB 686 21.008 40.509 3.185 1.00 22.19 ATOM 3823 CE1 PHE B 686 23.68941.003 3.714 1.00 22.33 ATOM 3824 CE2 PHE B 686 21.915 40.631 2.139 1.0023.22 ATOM 3825 CZ PHE B 686 23.259 40.882 2.406 1.00 22.45 ATOM 3826 CPHE B 686 20.017 43.025 5.345 1.00 19.33 ATOM 3827 O PHE B 686 20.92443.747 4.938 1.00 19.34 ATOM 3828 N ASP B 687 18.762 43.149 4.927 1.0020.18 ATOM 3829 CA ASP B 687 18.390 44.175 3.974 1.00 21.34 ATOM 3830 CBASP B 687 16.886 44.130 3.728 1.00 29.63 ATOM 3831 CG ASP B 687 16.42145.207 2.777 1.00 30.70 ATOM 3832 OD1 ASP B 687 16.880 45.210 1.616 1.0031.13 ATOM 3833 OD2 ASP B 687 15.602 46.053 3.194 1.00 32.12 ATOM 3834 CASP B 687 18.789 45.539 4.526 1.00 20.19 ATOM 3835 O ASP B 687 19.40246.344 3.826 1.00 20.58 ATOM 3836 N GLN B 688 18.447 45.779 5.790 1.0019.31 ATOM 3837 CA GLN B 688 18.773 47.044 6.447 1.00 20.14 ATOM 3838 CBGLN B 688 18.145 47.090 7.842 1.00 25.17 ATOM 3839 CG GLN B 688 16.62147.113 7.823 1.00 26.26 ATOM 3840 CD GLN B 688 16.074 48.399 7.241 1.0026.81 ATOM 3841 OE1 GLN B 688 16.218 49.471 7.835 1.00 28.04 ATOM 3842NE2 GLN B 688 15.456 48.306 6.071 1.00 26.91 ATOM 3843 C GLN B 68820.282 47.246 6.549 1.00 20.35 ATOM 3844 O GLN B 688 20.777 48.366 6.3891.00 19.51 ATOM 3845 N CYS B 689 21.003 46.159 6.811 1.00 19.79 ATOM3846 CA CYS B 689 22.457 46.199 6.924 1.00 20.08 ATOM 3847 CB CYS B 68922.984 44.803 7.271 1.00 19.48 ATOM 3848 SG CYS B 689 24.795 44.6637.336 1.00 17.52 ATOM 3849 C CYS B 689 23.085 46.679 5.617 1.00 19.76ATOM 3850 O CYS B 689 23.949 47.563 5.605 1.00 19.63 ATOM 3851 N LEU B690 22.655 46.072 4.517 1.00 19.56 ATOM 3852 CA LEU B 690 23.147 46.4173.192 1.00 20.27 ATOM 3853 CB LEU B 690 22.516 45.489 2.154 1.00 27.59ATOM 3854 CG LEU B 690 23.083 45.572 0.739 1.00 27.68 ATOM 3855 CD1 LEUB 690 24.542 45.123 0.746 1.00 28.21 ATOM 3856 CD2 LEU B 690 22.25744.692 −0.183 1.00 28.78 ATOM 3857 C LEU B 690 22.795 47.867 2.872 1.0020.36 ATOM 3858 O LEU B 690 23.607 48.606 2.332 1.00 21.09 ATOM 3859 NMET B 691 21.571 48.264 3.206 1.00 21.14 ATOM 3860 CA MET B 691 21.12049.630 2.961 1.00 22.00 ATOM 3861 CB MET B 691 19.730 49.839 3.568 1.0037.31 ATOM 3862 CG MET B 691 19.151 51.226 3.340 1.00 37.86 ATOM 3863 SDMET B 691 17.539 51.412 4.127 1.00 38.97 ATOM 3864 CE MET B 691 18.03051.835 5.809 1.00 38.00 ATOM 3865 C MET B 691 22.109 50.629 3.572 1.0022.35 ATOM 3866 O MET B 691 22.552 51.559 2.902 1.00 22.19 ATOM 3867 NILE B 692 22.455 50.420 4.839 1.00 21.40 ATOM 3868 CA ILE B 692 23.38551.308 5.534 1.00 21.97 ATOM 3869 CB ILE B 692 23.522 50.930 7.029 1.0025.90 ATOM 3870 CG2 ILE B 692 24.515 51.866 7.710 1.00 24.75 ATOM 3871CG1 ILE B 692 22.159 51.011 7.727 1.00 26.02 ATOM 3872 CD1 ILE B 69221.569 52.395 7.770 1.00 26.52 ATOM 3873 C ILE B 692 24.775 51.286 4.8991.00 22.83 ATOM 3874 O ILE B 692 25.391 52.332 4.704 1.00 21.06 ATOM3875 N LEU B 693 25.261 50.092 4.566 1.00 21.77 ATOM 3876 CA LEU B 69326.581 49.951 3.951 1.00 23.08 ATOM 3877 CB LEU B 693 26.940 48.4683.787 1.00 21.71 ATOM 3878 CG LEU B 693 27.301 47.701 5.060 1.00 21.98ATOM 3879 CD1 LEU B 693 27.277 46.218 4.784 1.00 22.22 ATOM 3880 CD2 LEUB 693 28.677 48.144 5.553 1.00 22.27 ATOM 3881 C LEU B 693 26.664 50.6352.595 1.00 23.02 ATOM 3882 O LEU B 693 27.752 51.009 2.153 1.00 24.07ATOM 3883 N ASN B 694 25.519 50.794 1.934 1.00 24.41 ATOM 3884 CA ASN B694 25.478 51.437 0.626 1.00 24.18 ATOM 3885 CB ASN B 694 24.448 50.760−0.285 1.00 28.06 ATOM 3886 CG ASN B 694 24.886 49.387 −0.756 1.00 28.56ATOM 3887 OD1 ASN B 694 26.040 49.184 −1.122 1.00 29.03 ATOM 3888 ND2ASN B 694 23.953 48.439 −0.769 1.00 28.87 ATOM 3889 C ASN B 694 25.14952.922 0.715 1.00 25.26 ATOM 3890 O ASN B 694 25.185 53.625 −0.295 1.0025.49 ATOM 3891 N SER B 695 24.830 53.392 1.917 1.00 24.51 ATOM 3892 CASER B 695 24.483 54.796 2.124 1.00 26.67 ATOM 3893 CB SER B 695 23.84254.991 3.497 1.00 38.96 ATOM 3894 OG SER B 695 22.544 54.433 3.532 1.0040.66 ATOM 3895 C SER B 695 25.679 55.724 1.999 1.00 26.23 ATOM 3896 OSER B 695 26.750 55.447 2.534 1.00 25.50 ATOM 3897 N PRO B 696 25.50356.854 1.298 1.00 30.83 ATOM 3898 CD PRO B 696 24.242 57.397 0.766 1.0035.10 ATOM 3899 CA PRO B 696 26.600 57.810 1.125 1.00 31.36 ATOM 3900 CBPRO B 696 25.936 58.959 0.362 1.00 35.40 ATOM 3901 CG PRO B 696 24.49958.882 0.813 1.00 35.60 ATOM 3902 C PRO B 696 27.205 58.251 2.461 1.0031.40 ATOM 3903 O PRO B 696 26.480 58.569 3.406 1.00 31.21 ATOM 3904 NGLY B 697 28.535 58.250 2.528 1.00 27.19 ATOM 3905 CA GLY B 697 29.22758.653 3.741 1.00 26.21 ATOM 3906 C GLY B 697 29.268 57.587 4.821 1.0025.99 ATOM 3907 O GLY B 697 29.813 57.811 5.901 1.00 25.64 ATOM 3908 NASN B 698 28.698 56.422 4.532 1.00 25.20 ATOM 3909 CA ASN B 698 28.66155.328 5.498 1.00 24.25 ATOM 3910 CB ASN B 698 27.215 54.970 5.867 1.0026.49 ATOM 3911 CG ASN B 698 26.516 56.050 6.651 1.00 26.36 ATOM 3912OD1 ASN B 698 26.081 57.067 6.101 1.00 28.19 ATOM 3913 ND2 ASN B 69826.399 55.834 7.948 1.00 26.66 ATOM 3914 C ASN B 698 29.302 54.053 4.9671.00 25.12 ATOM 3915 O ASN B 698 29.271 53.025 5.639 1.00 23.91 ATOM3916 N GLN B 699 29.876 54.114 3.771 1.00 24.45 ATOM 3917 CA GLN B 69930.456 52.923 3.146 1.00 24.83 ATOM 3918 CB GLN B 699 30.510 53.1431.633 1.00 34.19 ATOM 3919 CG GLN B 699 29.191 53.687 1.093 1.00 34.82ATOM 3920 CD GLN B 699 29.205 53.911 −0.399 1.00 35.20 ATOM 3921 OE1 GLNB 699 29.346 52.971 −1.178 1.00 35.77 ATOM 3922 NE2 GLN B 699 29.05655.163 −0.808 1.00 35.33 ATOM 3923 C GLN B 699 31.819 52.493 3.683 1.0023.99 ATOM 3924 O GLN B 699 32.860 52.768 3.083 1.00 25.36 ATOM 3925 NILE B 700 31.791 51.794 4.814 1.00 20.88 ATOM 3926 CA ILE B 700 32.99651.309 5.475 1.00 21.48 ATOM 3927 CB ILE B 700 32.696 50.857 6.919 1.0024.53 ATOM 3928 CG2 ILE B 700 32.254 52.056 7.759 1.00 24.80 ATOM 3929CG1 ILE B 700 31.623 49.765 6.917 1.00 24.49 ATOM 3930 CD1 ILE B 70031.415 49.110 8.268 1.00 24.76 ATOM 3931 C ILE B 700 33.674 50.154 4.7401.00 20.59 ATOM 3932 O ILE B 700 34.754 49.717 5.141 1.00 22.27 ATOM3933 N LEU B 701 33.051 49.665 3.669 1.00 23.58 ATOM 3934 CA LEU B 70133.627 48.571 2.892 1.00 23.94 ATOM 3935 CB LEU B 701 32.609 47.4332.711 1.00 22.71 ATOM 3936 CG LEU B 701 32.080 46.709 3.955 1.00 22.35ATOM 3937 CD1 LEU B 701 31.078 45.635 3.527 1.00 22.17 ATOM 3938 CD2 LEUB 701 33.235 46.087 4.732 1.00 22.94 ATOM 3939 C LEU B 701 34.058 49.0861.523 1.00 25.02 ATOM 3940 O LEU B 701 34.425 48.308 0.643 1.00 25.13ATOM 3941 N SER B 702 34.020 50.404 1.354 1.00 28.81 ATOM 3942 CA SER B702 34.383 51.035 0.087 1.00 30.23 ATOM 3943 CB SER B 702 34.177 52.5490.174 1.00 36.19 ATOM 3944 OG SER B 702 35.139 53.137 1.032 1.00 36.39ATOM 3945 C SER B 702 35.825 50.761 −0.323 1.00 30.61 ATOM 3946 O SER B702 36.154 50.788 −1.511 1.00 30.09 ATOM 3947 N GLY B 703 36.680 50.5040.661 1.00 30.88 ATOM 3948 CA GLY B 703 38.083 50.258 0.379 1.00 30.78ATOM 3949 C GLY B 703 38.446 48.843 −0.029 1.00 31.56 ATOM 3950 O GLY B703 39.570 48.595 −0.461 1.00 31.02 ATOM 3951 N LEU B 704 37.506 47.9140.109 1.00 27.62 ATOM 3952 CA LEU B 704 37.748 46.522 −0.252 1.00 28.14ATOM 3953 CB LEU B 704 36.638 45.628 0.312 1.00 24.97 ATOM 3954 CG LEU B704 36.734 45.205 1.775 1.00 25.06 ATOM 3955 CD1 LEU B 704 35.542 44.3492.161 1.00 25.71 ATOM 3956 CD2 LEU B 704 38.002 44.413 1.965 1.00 26.03ATOM 3957 C LEU B 704 37.834 46.306 −1.760 1.00 27.32 ATOM 3958 O LEU B704 37.211 47.026 −2.537 1.00 27.75 ATOM 3959 N SER B 705 38.610 45.305−2.164 1.00 25.03 ATOM 3960 CA SER B 705 38.740 44.982 −3.576 1.00 25.33ATOM 3961 CB SER B 705 39.909 44.019 −3.807 1.00 22.63 ATOM 3962 OG SERB 705 39.647 42.746 −3.249 1.00 22.15 ATOM 3963 C SER B 705 37.42844.308 −3.952 1.00 25.55 ATOM 3964 O SER B 705 36.645 43.950 −3.073 1.0025.89 ATOM 3965 N ILE B 706 37.190 44.134 −5.248 1.00 28.89 ATOM 3966 CAILE B 706 35.960 43.503 −5.712 1.00 30.40 ATOM 3967 CB ILE B 706 35.96743.351 −7.249 1.00 38.06 ATOM 3968 CG2 ILE B 706 34.756 42.548 −7.7011.00 38.45 ATOM 3969 CG1 ILE B 706 35.984 44.737 −7.900 1.00 38.67 ATOM3970 CD1 ILE B 706 36.141 44.717 −9.410 1.00 38.81 ATOM 3971 C ILE B 70635.735 42.134 −5.070 1.00 29.62 ATOM 3972 O ILE B 706 34.697 41.897−4.452 1.00 29.75 ATOM 3973 N GLU B 707 36.704 41.234 −5.210 1.00 26.84ATOM 3974 CA GLU B 707 36.579 39.900 −4.631 1.00 26.37 ATOM 3975 CB GLUB 707 37.811 39.056 −4.958 1.00 46.28 ATOM 3976 CG GLU B 707 37.66538.188 −6.198 1.00 47.22 ATOM 3977 CD GLU B 707 36.441 37.287 −6.1351.00 47.50 ATOM 3978 OE1 GLU B 707 35.368 37.699 −6.626 1.00 47.38 ATOM3979 OE2 GLU B 707 36.548 36.171 −5.581 1.00 47.48 ATOM 3980 C GLU B 70736.372 39.927 −3.121 1.00 25.62 ATOM 3981 O GLU B 707 35.505 39.227−2.591 1.00 24.84 ATOM 3982 N GLU B 708 37.175 40.723 −2.419 1.00 24.00ATOM 3983 CA GLU B 708 37.031 40.803 −0.974 1.00 22.95 ATOM 3984 CB GLUB 708 38.126 41.683 −0.365 1.00 34.88 ATOM 3985 CG GLU B 708 39.45140.952 −0.225 1.00 34.89 ATOM 3986 CD GLU B 708 40.418 41.646 0.714 1.0035.05 ATOM 3987 OE1 GLU B 708 41.368 40.981 1.167 1.00 35.66 ATOM 3988OE2 GLU B 708 40.235 42.846 0.994 1.00 35.78 ATOM 3989 C GLU B 70835.654 41.327 −0.579 1.00 23.54 ATOM 3990 O GLU B 708 35.049 40.8240.368 1.00 23.08 ATOM 3991 N TYR B 709 35.169 42.332 −1.302 1.00 22.88ATOM 3992 CA TYR B 709 33.855 42.908 −1.022 1.00 23.56 ATOM 3993 CB TYRB 709 33.583 44.072 −1.975 1.00 28.79 ATOM 3994 CG TYR B 709 32.22844.708 −1.784 1.00 29.56 ATOM 3995 CD1 TYR B 709 31.950 45.476 −0.6561.00 29.43 ATOM 3996 CE1 TYR B 709 30.691 46.039 −0.461 1.00 29.53 ATOM3997 CD2 TYR B 709 31.214 44.516 −2.718 1.00 30.32 ATOM 3998 CE2 TYR B709 29.950 45.072 −2.533 1.00 29.63 ATOM 3999 CZ TYR B 709 29.696 45.830−1.404 1.00 30.45 ATOM 4000 OH TYR B 709 28.447 46.375 −1.221 1.00 30.77ATOM 4001 C TYR B 709 32.764 41.841 −1.174 1.00 24.17 ATOM 4002 O TYR B709 31.909 41.677 −0.297 1.00 23.90 ATOM 4003 N LYS B 710 32.800 41.117−2.289 1.00 25.48 ATOM 4004 CA LYS B 710 31.821 40.062 −2.543 1.00 27.03ATOM 4005 CB LYS B 710 32.064 39.418 −3.910 1.00 49.22 ATOM 4006 CG LYSB 710 31.519 37.999 −3.992 1.00 50.09 ATOM 4007 CD LYS B 710 31.98537.258 −5.227 1.00 50.44 ATOM 4008 CE LYS B 710 31.769 35.762 −5.0571.00 50.21 ATOM 4009 NZ LYS B 710 30.379 35.439 −4.621 1.00 50.37 ATOM4010 C LYS B 710 31.872 38.972 −1.480 1.00 25.65 ATOM 4011 O LYS B 71030.840 38.500 −0.998 1.00 26.50 ATOM 4012 N THR B 711 33.081 38.556−1.128 1.00 23.83 ATOM 4013 CA THR B 711 33.249 37.511 −0.135 1.00 22.67ATOM 4014 CB THR B 711 34.727 37.120 −0.008 1.00 25.01 ATOM 4015 OG1 THRB 711 35.193 36.642 −1.275 1.00 25.50 ATOM 4016 CG2 THR B 711 34.90436.029 1.038 1.00 24.57 ATOM 4017 C THR B 711 32.723 37.944 1.232 1.0022.92 ATOM 4018 O THR B 711 32.095 37.157 1.940 1.00 23.60 ATOM 4019 NTHR B 712 32.975 39.202 1.586 1.00 20.46 ATOM 4020 CA THR B 712 32.55139.742 2.871 1.00 20.53 ATOM 4021 CB THR B 712 33.201 41.117 3.125 1.0022.65 ATOM 4022 OG1 THR B 712 34.624 40.993 3.023 1.00 23.36 ATOM 4023CG2 THR B 712 32.849 41.628 4.515 1.00 22.01 ATOM 4024 C THR B 71231.030 39.887 2.964 1.00 20.03 ATOM 4025 O THR B 712 30.433 39.564 3.9921.00 19.56 ATOM 4026 N LEU B 713 30.405 40.375 1.899 1.00 20.53 ATOM4027 CA LEU B 713 28.957 40.551 1.907 1.00 21.14 ATOM 4028 CB LEU B 71328.484 41.186 0.599 1.00 32.94 ATOM 4029 CG LEU B 713 27.729 42.5110.729 1.00 34.20 ATOM 4030 CD1 LEU B 713 26.628 42.370 1.774 1.00 34.24ATOM 4031 CD2 LEU B 713 28.684 43.616 1.134 1.00 34.00 ATOM 4032 C LEU B713 28.263 39.212 2.116 1.00 21.40 ATOM 4033 O LEU B 713 27.265 39.1172.834 1.00 19.21 ATOM 4034 N LYS B 714 28.795 38.171 1.488 1.00 20.01ATOM 4035 CA LYS B 714 28.220 36.837 1.620 1.00 20.38 ATOM 4036 CB LYS B714 28.920 35.876 0.657 1.00 40.77 ATOM 4037 CG LYS B 714 28.564 34.4190.847 1.00 41.45 ATOM 4038 CD LYS B 714 29.316 33.548 −0.149 1.00 42.11ATOM 4039 CE LYS B 714 29.138 32.073 0.165 1.00 42.05 ATOM 4040 NZ LYS B714 27.703 31.694 0.221 1.00 42.14 ATOM 4041 C LYS B 714 28.343 36.3223.052 1.00 19.95 ATOM 4042 O LYS B 714 27.417 35.721 3.597 1.00 20.70ATOM 4043 N ILE B 715 29.499 36.544 3.662 1.00 19.98 ATOM 4044 CA ILE B715 29.705 36.101 5.029 1.00 18.62 ATOM 4045 CB ILE B 715 31.145 36.3865.500 1.00 22.51 ATOM 4046 CG2 ILE B 715 31.317 35.943 6.939 1.00 21.50ATOM 4047 CG1 ILE B 715 32.141 35.638 4.612 1.00 22.82 ATOM 4048 CD1 ILEB 715 33.571 36.088 4.812 1.00 22.76 ATOM 4049 C ILE B 715 28.732 36.8385.955 1.00 18.65 ATOM 4050 O ILE B 715 28.190 36.245 6.882 1.00 17.75ATOM 4051 N ILE B 716 28.528 38.127 5.693 1.00 18.42 ATOM 4052 CA ILE B716 27.624 38.951 6.500 1.00 17.16 ATOM 4053 CB ILE B 716 27.676 40.4246.040 1.00 19.95 ATOM 4054 CG2 ILE B 716 26.549 41.225 6.683 1.00 19.27ATOM 4055 CG1 ILE B 716 29.037 41.024 6.404 1.00 18.80 ATOM 4056 CD1 ILEB 716 29.258 42.434 5.887 1.00 18.71 ATOM 4057 C ILE B 716 26.192 38.4266.411 1.00 19.67 ATOM 4058 O ILE B 716 25.544 38.183 7.436 1.00 16.84ATOM 4059 N LYS B 717 25.706 38.224 5.192 1.00 17.44 ATOM 4060 CA LYS B717 24.344 37.721 5.040 1.00 19.23 ATOM 4061 CB LYS B 717 23.980 37.4893.573 1.00 19.08 ATOM 4062 CG LYS B 717 22.575 36.915 3.425 1.00 19.36ATOM 4063 CD LYS B 717 22.145 36.779 1.975 1.00 20.95 ATOM 4064 CE LYS B717 20.713 36.253 1.906 1.00 20.68 ATOM 4065 NZ LYS B 717 20.177 36.2450.520 1.00 22.57 ATOM 4066 C LYS B 717 24.167 36.408 5.797 1.00 18.60ATOM 4067 O LYS B 717 23.204 36.240 6.539 1.00 19.65 ATOM 4068 N GLN B718 25.091 35.469 5.602 1.00 18.67 ATOM 4069 CA GLN B 718 24.992 34.1816.280 1.00 18.42 ATOM 4070 CB GLN B 718 26.110 33.256 5.794 1.00 35.34ATOM 4071 CG GLN B 718 25.885 32.724 4.386 1.00 36.06 ATOM 4072 CD GLN B718 27.121 32.072 3.798 1.00 36.81 ATOM 4073 OE1 GLN B 718 27.036 31.2952.843 1.00 37.02 ATOM 4074 NE2 GLN B 718 28.282 32.397 4.356 1.00 36.65ATOM 4075 C GLN B 718 25.039 34.298 7.802 1.00 16.64 ATOM 4076 O GLN B718 24.337 33.577 8.517 1.00 17.20 ATOM 4077 N ALA B 719 25.855 35.2218.299 1.00 17.42 ATOM 4078 CA ALA B 719 25.989 35.400 9.737 1.00 16.91ATOM 4079 CB ALA B 719 27.181 36.314 10.037 1.00 18.95 ATOM 4080 C ALA B719 24.705 35.979 10.338 1.00 16.46 ATOM 4081 O ALA B 719 24.280 35.56611.415 1.00 16.41 ATOM 4082 N ILE B 720 24.087 36.923 9.632 1.00 16.16ATOM 4083 CA ILE B 720 22.848 37.517 10.128 1.00 18.05 ATOM 4084 CB ILEB 720 22.463 38.775 9.317 1.00 16.77 ATOM 4085 CG2 ILE B 720 21.02139.200 9.634 1.00 17.00 ATOM 4086 CG1 ILE B 720 23.458 39.903 9.626 1.0017.24 ATOM 4087 CD1 ILE B 720 23.165 41.216 8.938 1.00 18.75 ATOM 4088 CILE B 720 21.725 36.484 10.083 1.00 16.85 ATOM 4089 O ILE B 720 20.96636.339 11.044 1.00 17.13 ATOM 4090 N LEU B 721 21.628 35.741 8.983 1.0017.26 ATOM 4091 CA LEU B 721 20.588 34.726 8.886 1.00 17.99 ATOM 4092 CBLEU B 721 20.611 34.056 7.507 1.00 21.38 ATOM 4093 CG LEU B 721 19.99834.910 6.390 1.00 22.95 ATOM 4094 CD1 LEU B 721 20.102 34.181 5.071 1.0022.96 ATOM 4095 CD2 LEU B 721 18.544 35.204 6.707 1.00 22.88 ATOM 4096 CLEU B 721 20.764 33.686 9.984 1.00 17.50 ATOM 4097 O LEU B 721 19.79133.142 10.493 1.00 18.24 ATOM 4098 N ALA B 722 22.013 33.425 10.359 1.0018.93 ATOM 4099 CA ALA B 722 22.305 32.448 11.398 1.00 19.70 ATOM 4100CB ALA B 722 23.818 32.282 11.556 1.00 22.76 ATOM 4101 C ALA B 72221.689 32.803 12.748 1.00 19.06 ATOM 4102 O ALA B 722 21.491 31.92613.581 1.00 19.32 ATOM 4103 N THR B 723 21.389 34.081 12.972 1.00 19.12ATOM 4104 CA THR B 723 20.820 34.484 14.255 1.00 18.93 ATOM 4105 CB THRB 723 20.997 36.000 14.503 1.00 16.46 ATOM 4106 OG1 THR B 723 20.35936.746 13.463 1.00 18.08 ATOM 4107 CG2 THR B 723 22.485 36.355 14.5361.00 17.70 ATOM 4108 C THR B 723 19.352 34.093 14.440 1.00 20.30 ATOM4109 O THR B 723 18.744 34.373 15.474 1.00 18.88 ATOM 4110 N ASP B 72418.785 33.464 13.421 1.00 20.75 ATOM 4111 CA ASP B 724 17.417 32.97713.495 1.00 21.45 ATOM 4112 CB ASP B 724 16.901 32.670 12.084 1.00 20.47ATOM 4113 CG ASP B 724 15.541 31.991 12.091 1.00 19.47 ATOM 4114 OD1 ASPB 724 14.982 31.769 13.183 1.00 20.37 ATOM 4115 OD2 ASP B 724 15.02931.683 10.995 1.00 20.97 ATOM 4116 C ASP B 724 17.571 31.684 14.296 1.0022.80 ATOM 4117 O ASP B 724 18.171 30.729 13.803 1.00 21.11 ATOM 4118 NLEU B 725 17.057 31.648 15.524 1.00 21.88 ATOM 4119 CA LEU B 725 17.21130.454 16.354 1.00 23.26 ATOM 4120 CB LEU B 725 16.575 30.659 17.7341.00 21.15 ATOM 4121 CG LEU B 725 17.439 31.482 18.698 1.00 22.29 ATOM4122 CD1 LEU B 725 16.712 31.674 20.019 1.00 22.69 ATOM 4123 CD2 LEU B725 18.768 30.765 18.927 1.00 22.08 ATOM 4124 C LEU B 725 16.685 29.17815.720 1.00 24.43 ATOM 4125 O LEU B 725 17.084 28.074 16.110 1.00 24.43ATOM 4126 N ALA B 726 15.802 29.322 14.735 1.00 24.46 ATOM 4127 CA ALA B726 15.256 28.158 14.042 1.00 24.85 ATOM 4128 CB ALA B 726 14.096 28.57613.144 1.00 26.10 ATOM 4129 C ALA B 726 16.361 27.502 13.219 1.00 25.58ATOM 4130 O ALA B 726 16.436 26.277 13.127 1.00 24.81 ATOM 4131 N LEU B727 17.217 28.323 12.617 1.00 25.66 ATOM 4132 CA LEU B 727 18.332 27.82611.825 1.00 26.45 ATOM 4133 CB LEU B 727 18.952 28.969 11.016 1.00 32.52ATOM 4134 CG LEU B 727 18.730 28.953 9.499 1.00 34.10 ATOM 4135 CD1 LEUB 727 17.320 28.490 9.163 1.00 32.76 ATOM 4136 CD2 LEU B 727 18.99930.343 8.938 1.00 32.91 ATOM 4137 C LEU B 727 19.370 27.216 12.767 1.0026.66 ATOM 4138 O LEU B 727 19.994 26.208 12.448 1.00 27.25 ATOM 4139 NTYR B 728 19.549 27.828 13.933 1.00 23.88 ATOM 4140 CA TYR B 728 20.49727.311 14.912 1.00 24.96 ATOM 4141 CB TYR B 728 20.576 28.246 16.1271.00 22.32 ATOM 4142 CG TYR B 728 21.197 27.606 17.348 1.00 22.57 ATOM4143 CD1 TYR B 728 20.402 27.173 18.410 1.00 23.27 ATOM 4144 CE1 TYR B728 20.958 26.520 19.512 1.00 22.36 ATOM 4145 CD2 TYR B 728 22.56927.372 17.416 1.00 23.33 ATOM 4146 CE2 TYR B 728 23.133 26.713 18.5121.00 22.71 ATOM 4147 CZ TYR B 728 22.322 26.292 19.553 1.00 23.34 ATOM4148 OH TYR B 728 22.876 25.642 20.638 1.00 25.15 ATOM 4149 C TYR B 72820.085 25.908 15.365 1.00 25.55 ATOM 4150 O TYR B 728 20.894 24.98215.368 1.00 25.79 ATOM 4151 N ILE B 729 18.821 25.759 15.747 1.00 27.10ATOM 4152 CA ILE B 729 18.313 24.476 16.218 1.00 27.90 ATOM 4153 CB ILEB 729 16.849 24.608 16.692 1.00 33.37 ATOM 4154 CG2 ILE B 729 16.24523.231 16.936 1.00 34.11 ATOM 4155 CG1 ILE B 729 16.800 25.447 17.9691.00 33.59 ATOM 4156 CD1 ILE B 729 15.400 25.662 18.512 1.00 34.44 ATOM4157 C ILE B 729 18.396 23.395 15.151 1.00 28.43 ATOM 4158 O ILE B 72918.561 22.212 15.463 1.00 28.49 ATOM 4159 N LYS B 730 18.286 23.80313.893 1.00 30.10 ATOM 4160 CA LYS B 730 18.335 22.865 12.777 1.00 30.87ATOM 4161 CB LYS B 730 17.637 23.474 11.554 1.00 41.47 ATOM 4162 CG LYSB 730 17.736 22.627 10.292 1.00 41.83 ATOM 4163 CD LYS B 730 17.08223.312 9.099 1.00 41.85 ATOM 4164 CE LYS B 730 17.161 22.437 7.856 1.0042.29 ATOM 4165 NZ LYS B 730 16.471 23.056 6.689 1.00 41.92 ATOM 4166 CLYS B 730 19.753 22.450 12.390 1.00 30.30 ATOM 4167 O LYS B 730 19.96821.341 11.899 1.00 30.78 ATOM 4168 N ARG B 731 20.722 23.330 12.611 1.0026.44 ATOM 4169 CA ARG B 731 22.101 23.029 12.234 1.00 26.05 ATOM 4170CB ARG B 731 22.691 24.207 11.455 1.00 44.87 ATOM 4171 CG ARG B 73122.027 24.477 10.123 1.00 45.35 ATOM 4172 CD ARG B 731 22.579 25.7399.481 1.00 45.70 ATOM 4173 NE ARG B 731 24.018 25.666 9.236 1.00 45.72ATOM 4174 CZ ARG B 731 24.600 24.771 8.445 1.00 45.64 ATOM 4175 NH1 ARGB 731 23.870 23.859 7.816 1.00 45.97 ATOM 4176 NH2 ARG B 731 25.91524.793 8.272 1.00 45.83 ATOM 4177 C ARG B 731 23.076 22.657 13.349 1.0025.87 ATOM 4178 O ARG B 731 24.144 22.121 13.069 1.00 25.60 ATOM 4179 NARG B 732 22.724 22.931 14.600 1.00 24.75 ATOM 4180 CA ARG B 732 23.63622.646 15.704 1.00 24.59 ATOM 4181 CB ARG B 732 23.051 23.154 17.0211.00 28.71 ATOM 4182 CG ARG B 732 21.825 22.412 17.490 1.00 28.36 ATOM4183 CD ARG B 732 21.266 23.052 18.742 1.00 28.99 ATOM 4184 NE ARG B 73220.160 22.282 19.295 1.00 28.09 ATOM 4185 CZ ARG B 732 19.555 22.56720.444 1.00 29.06 ATOM 4186 NH1 ARG B 732 19.951 23.607 21.164 1.0029.87 ATOM 4187 NH2 ARG B 732 18.560 21.807 20.878 1.00 29.81 ATOM 4188C ARG B 732 24.027 21.177 15.845 1.00 24.59 ATOM 4189 O ARG B 732 25.14320.871 16.272 1.00 24.56 ATOM 4190 N GLY B 733 23.114 20.278 15.495 1.0028.28 ATOM 4191 CA GLY B 733 23.409 18.857 15.592 1.00 29.55 ATOM 4192 CGLY B 733 24.686 18.506 14.852 1.00 29.73 ATOM 4193 O GLY B 733 25.58217.856 15.402 1.00 29.54 ATOM 4194 N GLU B 734 24.775 18.940 13.599 1.0029.63 ATOM 4195 CA GLU B 734 25.954 18.676 12.779 1.00 29.74 ATOM 4196CB GLU B 734 25.772 19.317 11.396 1.00 37.09 ATOM 4197 CG GLU B 73427.011 19.313 10.513 1.00 37.69 ATOM 4198 CD GLU B 734 26.712 19.7499.090 1.00 37.69 ATOM 4199 OE1 GLU B 734 25.895 20.673 8.905 1.00 37.77ATOM 4200 OE2 GLU B 734 27.302 19.174 8.153 1.00 37.96 ATOM 4201 C GLU B734 27.234 19.187 13.448 1.00 29.89 ATOM 4202 O GLU B 734 28.241 18.48113.508 1.00 29.99 ATOM 4203 N PHE B 735 27.193 20.416 13.953 1.00 26.19ATOM 4204 CA PHE B 735 28.348 21.015 14.617 1.00 28.01 ATOM 4205 CB PHEB 735 28.001 22.449 15.051 1.00 32.46 ATOM 4206 CG PHE B 735 29.12123.170 15.748 1.00 32.58 ATOM 4207 CD1 PHE B 735 30.350 23.353 15.1211.00 32.98 ATOM 4208 CD2 PHE B 735 28.930 23.710 17.018 1.00 32.86 ATOM4209 CE1 PHE B 735 31.374 24.067 15.746 1.00 33.43 ATOM 4210 CE2 PHE B735 29.941 24.424 17.653 1.00 33.17 ATOM 4211 CZ PHE B 735 31.168 24.60617.017 1.00 33.32 ATOM 4212 C PHE B 735 28.759 20.185 15.832 1.00 28.38ATOM 4213 O PHE B 735 29.943 19.877 16.023 1.00 28.13 ATOM 4214 N PHE B736 27.772 19.823 16.646 1.00 35.56 ATOM 4215 CA PHE B 736 28.008 19.03317.848 1.00 36.50 ATOM 4216 CB PHE B 736 26.695 18.843 18.615 1.00 29.57ATOM 4217 CG PHE B 736 26.153 20.118 19.217 1.00 28.48 ATOM 4218 CD1 PHEB 736 24.849 20.174 19.707 1.00 29.25 ATOM 4219 CD2 PHE B 736 26.94721.261 19.298 1.00 28.68 ATOM 4220 CE1 PHE B 736 24.343 21.351 20.2701.00 28.48 ATOM 4221 CE2 PHE B 736 26.451 22.440 19.857 1.00 28.64 ATOM4222 CZ PHE B 736 25.142 22.481 20.344 1.00 28.27 ATOM 4223 C PHE B 73628.636 17.678 17.538 1.00 36.98 ATOM 4224 O PHE B 736 29.472 17.19218.299 1.00 37.51 ATOM 4225 N GLU B 737 28.236 17.074 16.422 1.00 35.33ATOM 4226 CA GLU B 737 28.779 15.778 16.019 1.00 34.66 ATOM 4227 CB GLUB 737 28.042 15.245 14.788 1.00 48.23 ATOM 4228 CG GLU B 737 26.62414.782 15.052 1.00 48.59 ATOM 4229 CD GLU B 737 26.562 13.677 16.0841.00 48.98 ATOM 4230 OE1 GLU B 737 27.347 12.710 15.969 1.00 48.80 ATOM4231 OE2 GLU B 737 25.724 13.771 17.004 1.00 49.04 ATOM 4232 C GLU B 73730.264 15.895 15.698 1.00 35.25 ATOM 4233 O GLU B 737 31.095 15.18416.276 1.00 34.50 ATOM 4234 N LEU B 738 30.582 16.792 14.766 1.00 34.53ATOM 4235 CA LEU B 738 31.958 17.036 14.339 1.00 34.99 ATOM 4236 CB LEUB 738 32.010 18.266 13.422 1.00 33.43 ATOM 4237 CG LEU B 738 31.53218.137 11.969 1.00 33.44 ATOM 4238 CD1 LEU B 738 30.237 17.345 11.8851.00 33.77 ATOM 4239 CD2 LEU B 738 31.345 19.531 11.388 1.00 33.47 ATOM4240 C LEU B 738 32.889 17.243 15.530 1.00 35.52 ATOM 4241 O LEU B 73834.020 16.760 15.535 1.00 35.19 ATOM 4242 N ILE B 739 32.403 17.96016.538 1.00 35.96 ATOM 4243 CA ILE B 739 33.177 18.243 17.740 1.00 36.59ATOM 4244 CB ILE B 739 32.489 19.347 18.578 1.00 41.13 ATOM 4245 CG2 ILEB 739 33.192 19.509 19.913 1.00 41.32 ATOM 4246 CG1 ILE B 739 32.47820.665 17.798 1.00 41.45 ATOM 4247 CD1 ILE B 739 33.852 21.224 17.5101.00 41.21 ATOM 4248 C ILE B 739 33.353 16.998 18.610 1.00 37.53 ATOM4249 O ILE B 739 34.455 16.711 19.088 1.00 36.85 ATOM 4250 N ARG B 74032.262 16.264 18.808 1.00 40.80 ATOM 4251 CA ARG B 740 32.276 15.05819.627 1.00 41.57 ATOM 4252 CB ARG B 740 30.860 14.490 19.744 1.00 49.23ATOM 4253 CG ARG B 740 30.708 13.372 20.763 1.00 49.50 ATOM 4254 CD ARGB 740 29.268 12.894 20.816 1.00 49.76 ATOM 4255 NE ARG B 740 28.87012.228 19.577 1.00 49.63 ATOM 4256 CZ ARG B 740 29.192 10.977 19.2641.00 49.97 ATOM 4257 NH1 ARG B 740 29.917 10.246 20.103 1.00 49.93 ATOM4258 NH2 ARG B 740 28.795 10.456 18.111 1.00 49.81 ATOM 4259 C ARG B 74033.202 13.999 19.045 1.00 41.31 ATOM 4260 O ARG B 740 34.041 13.43719.750 1.00 41.75 ATOM 4261 N LYS B 741 33.048 13.734 17.753 1.00 36.01ATOM 4262 CA LYS B 741 33.858 12.734 17.074 1.00 36.04 ATOM 4263 CB LYSB 741 33.142 12.261 15.806 1.00 51.86 ATOM 4264 CG LYS B 741 31.82311.547 16.084 1.00 52.33 ATOM 4265 CD LYS B 741 31.198 10.984 14.8191.00 52.60 ATOM 4266 CE LYS B 741 29.956 10.164 15.147 1.00 52.72 ATOM4267 NZ LYS B 741 29.371 9.514 13.941 1.00 52.84 ATOM 4268 C LYS B 74135.257 13.229 16.739 1.00 36.83 ATOM 4269 O LYS B 741 36.017 12.54416.056 1.00 35.76 ATOM 4270 N ASN B 742 35.598 14.424 17.217 1.00 47.96ATOM 4271 CA ASN B 742 36.925 14.991 16.979 1.00 48.89 ATOM 4272 CB ASNB 742 37.984 14.073 17.601 1.00 45.18 ATOM 4273 CG ASN B 742 37.66013.696 19.038 1.00 45.25 ATOM 4274 OD1 ASN B 742 37.873 14.481 19.9581.00 45.19 ATOM 4275 ND2 ASN B 742 37.127 12.492 19.231 1.00 45.61 ATOM4276 C ASN B 742 37.210 15.160 15.482 1.00 48.30 ATOM 4277 O ASN B 74238.318 14.886 15.023 1.00 49.56 ATOM 4278 N GLN B 743 36.214 15.62714.733 1.00 35.63 ATOM 4279 CA GLN B 743 36.345 15.806 13.288 1.00 33.02ATOM 4280 CB GLN B 743 35.226 15.034 12.583 1.00 55.29 ATOM 4281 CG GLNB 743 34.914 13.679 13.206 1.00 55.90 ATOM 4282 CD GLN B 743 33.53113.159 12.830 1.00 56.30 ATOM 4283 OE1 GLN B 743 32.531 13.872 12.9431.00 56.03 ATOM 4284 NE2 GLN B 743 33.470 11.903 12.396 1.00 56.30 ATOM4285 C GLN B 743 36.296 17.272 12.833 1.00 32.63 ATOM 4286 O GLN B 74336.519 17.568 11.659 1.00 30.98 ATOM 4287 N PHE B 744 36.008 18.18613.754 1.00 30.07 ATOM 4288 CA PHE B 744 35.913 19.600 13.396 1.00 29.86ATOM 4289 CB PHE B 744 35.664 20.451 14.646 1.00 36.04 ATOM 4290 CG PHEB 744 35.433 21.906 14.349 1.00 36.02 ATOM 4291 CD1 PHE B 744 34.42622.294 13.472 1.00 36.51 ATOM 4292 CD2 PHE B 744 36.224 22.886 14.9391.00 36.37 ATOM 4293 CE1 PHE B 744 34.210 23.641 13.186 1.00 36.33 ATOM4294 CE2 PHE B 744 36.017 24.237 14.660 1.00 36.35 ATOM 4295 CZ PHE B744 35.007 24.613 13.781 1.00 36.44 ATOM 4296 C PHE B 744 37.158 20.10112.671 1.00 30.17 ATOM 4297 O PHE B 744 38.274 19.948 13.163 1.00 29.71ATOM 4298 N ASN B 745 36.953 20.703 11.500 1.00 33.40 ATOM 4299 CA ASN B745 38.047 21.229 10.685 1.00 34.97 ATOM 4300 CB ASN B 745 38.463 20.1929.634 1.00 36.63 ATOM 4301 CG ASN B 745 39.397 20.765 8.586 1.00 36.73ATOM 4302 OD1 ASN B 745 40.281 21.562 8.896 1.00 37.02 ATOM 4303 ND2 ASNB 745 39.216 20.345 7.337 1.00 37.05 ATOM 4304 C ASN B 745 37.674 22.5379.992 1.00 34.71 ATOM 4305 O ASN B 745 36.930 22.540 9.011 1.00 34.81ATOM 4306 N LEU B 746 38.209 23.645 10.495 1.00 32.32 ATOM 4307 CA LEU B746 37.914 24.961 9.934 1.00 31.51 ATOM 4308 CB LEU B 746 38.459 26.05910.853 1.00 35.95 ATOM 4309 CG LEU B 746 37.591 26.325 12.083 1.00 36.41ATOM 4310 CD1 LEU B 746 38.239 27.390 12.951 1.00 36.26 ATOM 4311 CD2LEU B 746 36.200 26.773 11.635 1.00 36.10 ATOM 4312 C LEU B 746 38.41925.181 8.511 1.00 31.36 ATOM 4313 O LEU B 746 38.085 26.183 7.877 1.0031.04 ATOM 4314 N GLU B 747 39.224 24.252 8.010 1.00 30.95 ATOM 4315 CAGLU B 747 39.738 24.357 6.650 1.00 31.86 ATOM 4316 CB GLU B 747 40.91823.402 6.453 1.00 51.07 ATOM 4317 CG GLU B 747 42.129 23.738 7.311 1.0051.73 ATOM 4318 CD GLU B 747 43.251 22.728 7.163 1.00 52.11 ATOM 4319OE1 GLU B 747 43.666 22.467 6.014 1.00 52.03 ATOM 4320 OE2 GLU B 74743.718 22.201 8.196 1.00 52.21 ATOM 4321 C GLU B 747 38.617 24.014 5.6701.00 31.25 ATOM 4322 O GLU B 747 38.646 24.421 4.507 1.00 30.95 ATOM4323 N ASP B 748 37.634 23.260 6.156 1.00 31.79 ATOM 4324 CA ASP B 74836.480 22.864 5.357 1.00 31.93 ATOM 4325 CB ASP B 748 35.754 21.6976.031 1.00 39.97 ATOM 4326 CG ASP B 748 34.571 21.193 5.223 1.00 40.51ATOM 4327 OD1 ASP B 748 33.678 21.995 4.889 1.00 40.27 ATOM 4328 OD2 ASPB 748 34.533 19.981 4.928 1.00 40.36 ATOM 4329 C ASP B 748 35.546 24.0715.265 1.00 32.12 ATOM 4330 O ASP B 748 35.026 24.538 6.280 1.00 31.68ATOM 4331 N PRO B 749 35.317 24.586 4.046 1.00 30.33 ATOM 4332 CD PRO B749 35.694 23.972 2.761 1.00 44.68 ATOM 4333 CA PRO B 749 34.445 25.7463.827 1.00 30.40 ATOM 4334 CB PRO B 749 34.380 25.845 2.304 1.00 44.80ATOM 4335 CG PRO B 749 34.577 24.423 1.863 1.00 45.23 ATOM 4336 C PRO B749 33.065 25.626 4.470 1.00 30.78 ATOM 4337 O PRO B 749 32.553 26.5915.045 1.00 29.64 ATOM 4338 N HIS B 750 32.464 24.443 4.379 1.00 31.42ATOM 4339 CA HIS B 750 31.148 24.231 4.963 1.00 31.75 ATOM 4340 CB HIS B750 30.569 22.890 4.513 1.00 36.05 ATOM 4341 CG HIS B 750 29.289 22.5295.200 1.00 36.27 ATOM 4342 CD2 HIS B 750 28.002 22.836 4.908 1.00 35.87ATOM 4343 ND1 HIS B 750 29.250 21.786 6.360 1.00 36.16 ATOM 4344 CE1 HISB 750 27.996 21.648 6.752 1.00 36.46 ATOM 4345 NE2 HIS B 750 27.21922.276 5.888 1.00 36.37 ATOM 4346 C HIS B 750 31.212 24.288 6.480 1.0031.05 ATOM 4347 O HIS B 750 30.373 24.922 7.118 1.00 31.52 ATOM 4348 NGLU B 751 32.208 23.629 7.062 1.00 26.46 ATOM 4349 CA GLU B 751 32.35623.642 8.512 1.00 26.08 ATOM 4350 CB GLU B 751 33.415 22.625 8.946 1.0032.16 ATOM 4351 CG GLU B 751 33.004 21.185 8.700 1.00 32.81 ATOM 4352 CDGLU B 751 34.040 20.193 9.190 1.00 32.54 ATOM 4353 OE1 GLU B 751 34.38120.234 10.392 1.00 32.25 ATOM 4354 OE2 GLU B 751 34.507 19.373 8.3721.00 33.04 ATOM 4355 C GLU B 751 32.741 25.038 8.997 1.00 25.23 ATOM4356 O GLU B 751 32.426 25.424 10.127 1.00 26.00 ATOM 4357 N LYS B 75233.413 25.791 8.134 1.00 25.46 ATOM 4358 CA LYS B 752 33.835 27.1448.477 1.00 25.14 ATOM 4359 CB LYS B 752 34.760 27.710 7.400 1.00 34.00ATOM 4360 CG LYS B 752 35.473 28.988 7.807 1.00 34.35 ATOM 4361 CD LYS B752 36.445 28.715 8.950 1.00 34.98 ATOM 4362 CE LYS B 752 37.386 29.8789.166 1.00 34.20 ATOM 4363 NZ LYS B 752 38.098 30.208 7.910 1.00 34.22ATOM 4364 C LYS B 752 32.600 28.024 8.593 1.00 25.44 ATOM 4365 O LYS B752 32.435 28.747 9.574 1.00 25.14 ATOM 4366 N GLU B 753 31.724 27.9567.597 1.00 26.17 ATOM 4367 CA GLU B 753 30.519 28.775 7.639 1.00 27.32ATOM 4368 CB GLU B 753 29.773 28.743 6.300 1.00 47.16 ATOM 4369 CG GLU B753 29.010 27.468 6.008 1.00 48.02 ATOM 4370 CD GLU B 753 28.190 27.5784.738 1.00 48.29 ATOM 4371 OE1 GLU B 753 28.791 27.692 3.647 1.00 48.21ATOM 4372 OE2 GLU B 753 26.944 27.561 4.832 1.00 48.25 ATOM 4373 C GLU B753 29.620 28.287 8.764 1.00 26.46 ATOM 4374 O GLU B 753 28.913 29.0809.383 1.00 26.43 ATOM 4375 N LEU B 754 29.658 26.983 9.035 1.00 24.18ATOM 4376 CA LEU B 754 28.860 26.406 10.110 1.00 22.29 ATOM 4377 CB LEUB 754 28.981 24.877 10.116 1.00 25.44 ATOM 4378 CG LEU B 754 28.26424.173 11.273 1.00 25.42 ATOM 4379 CD1 LEU B 754 26.772 24.485 11.2341.00 26.03 ATOM 4380 CD2 LEU B 754 28.494 22.674 11.174 1.00 26.23 ATOM4381 C LEU B 754 29.338 26.957 11.451 1.00 22.78 ATOM 4382 O LEU B 75428.524 27.323 12.308 1.00 23.06 ATOM 4383 N PHE B 755 30.657 27.01511.636 1.00 20.22 ATOM 4384 CA PHE B 755 31.216 27.528 12.872 1.00 20.52ATOM 4385 CB PHE B 755 32.745 27.445 12.870 1.00 21.28 ATOM 4386 CG PHEB 755 33.380 28.142 14.042 1.00 20.97 ATOM 4387 CD1 PHE B 755 33.21227.654 15.332 1.00 21.53 ATOM 4388 CD2 PHE B 755 34.111 29.309 13.8581.00 22.19 ATOM 4389 CE1 PHE B 755 33.763 28.323 16.426 1.00 21.26 ATOM4390 CE2 PHE B 755 34.667 29.989 14.949 1.00 21.93 ATOM 4391 CZ PHE B755 34.492 29.496 16.230 1.00 21.53 ATOM 4392 C PHE B 755 30.811 28.98213.064 1.00 19.98 ATOM 4393 O PHE B 755 30.378 29.372 14.147 1.00 22.32ATOM 4394 N LEU B 756 30.968 29.778 12.010 1.00 19.82 ATOM 4395 CA LEU B756 30.621 31.193 12.070 1.00 19.75 ATOM 4396 CB LEU B 756 30.868 31.85810.716 1.00 18.84 ATOM 4397 CG LEU B 756 32.329 31.854 10.252 1.00 18.79ATOM 4398 CD1 LEU B 756 32.433 32.482 8.864 1.00 19.24 ATOM 4399 CD2 LEUB 756 33.192 32.610 11.262 1.00 19.62 ATOM 4400 C LEU B 756 29.16531.372 12.488 1.00 21.11 ATOM 4401 O LEU B 756 28.839 32.294 13.233 1.0019.94 ATOM 4402 N ALA B 757 28.291 30.488 12.014 1.00 20.80 ATOM 4403 CAALA B 757 26.873 30.568 12.373 1.00 21.25 ATOM 4404 CB ALA B 757 26.06429.560 11.552 1.00 23.40 ATOM 4405 C ALA B 757 26.693 30.294 13.861 1.0022.25 ATOM 4406 O ALA B 757 25.917 30.971 14.542 1.00 22.17 ATOM 4407 NMET B 758 27.412 29.291 14.364 1.00 19.96 ATOM 4408 CA MET B 758 27.34828.926 15.771 1.00 20.73 ATOM 4409 CB MET B 758 28.154 27.647 16.0231.00 27.97 ATOM 4410 CG MET B 758 27.601 26.422 15.324 1.00 27.07 ATOM4411 SD MET B 758 25.940 25.980 15.881 1.00 27.12 ATOM 4412 CE MET B 75824.971 26.627 14.530 1.00 27.43 ATOM 4413 C MET B 758 27.895 30.04316.656 1.00 18.82 ATOM 4414 O MET B 758 27.352 30.315 17.725 1.00 21.47ATOM 4415 N LEU B 759 28.976 30.674 16.208 1.00 19.71 ATOM 4416 CA LEU B759 29.597 31.756 16.954 1.00 18.16 ATOM 4417 CB LEU B 759 30.892 32.18916.270 1.00 20.33 ATOM 4418 CG LEU B 759 31.646 33.349 16.919 1.00 19.85ATOM 4419 CD1 LEU B 759 31.992 33.005 18.363 1.00 21.09 ATOM 4420 CD2LEU B 759 32.891 33.646 16.103 1.00 19.80 ATOM 4421 C LEU B 759 28.63532.933 17.048 1.00 20.05 ATOM 4422 O LEU B 759 28.535 33.577 18.091 1.0019.37 ATOM 4423 N MET B 760 27.921 33.202 15.960 1.00 18.13 ATOM 4424 CAMET B 760 26.955 34.302 15.959 1.00 19.70 ATOM 4425 CB MET B 760 26.32534.455 14.575 1.00 17.26 ATOM 4426 CG MET B 760 27.211 35.177 13.5471.00 16.88 ATOM 4427 SD MET B 760 27.567 36.936 13.895 1.00 17.69 ATOM4428 CE MET B 760 25.887 37.644 13.962 1.00 17.02 ATOM 4429 C MET B 76025.879 34.059 17.017 1.00 18.46 ATOM 4430 O MET B 760 25.510 34.97017.765 1.00 18.74 ATOM 4431 N THR B 761 25.380 32.831 17.102 1.00 17.88ATOM 4432 CA THR B 761 24.358 32.516 18.092 1.00 17.90 ATOM 4433 CB THRB 761 23.858 31.070 17.933 1.00 20.06 ATOM 4434 OG1 THR B 761 23.31630.905 16.619 1.00 20.01 ATOM 4435 CG2 THR B 761 22.778 30.746 18.9711.00 19.13 ATOM 4436 C THR B 761 24.922 32.694 19.495 1.00 18.35 ATOM4437 O THR B 761 24.265 33.241 20.375 1.00 17.84 ATOM 4438 N ALA B 76226.160 32.244 19.695 1.00 18.42 ATOM 4439 CA ALA B 762 26.808 32.34720.996 1.00 17.98 ATOM 4440 CB ALA B 762 28.224 31.780 20.930 1.00 19.48ATOM 4441 C ALA B 762 26.843 33.795 21.472 1.00 17.59 ATOM 4442 O ALA B762 26.567 34.077 22.637 1.00 20.01 ATOM 4443 N CYS B 763 27.186 34.70520.570 1.00 17.78 ATOM 4444 CA CYS B 763 27.247 36.115 20.914 1.00 18.49ATOM 4445 CB CYS B 763 28.041 36.869 19.850 1.00 20.27 ATOM 4446 SG CYSB 763 29.790 36.353 19.790 1.00 21.15 ATOM 4447 C CYS B 763 25.84136.704 21.071 1.00 19.17 ATOM 4448 O CYS B 763 25.596 37.521 21.957 1.0019.53 ATOM 4449 N ASP B 764 24.921 36.265 20.219 1.00 20.39 ATOM 4450 CAASP B 764 23.534 36.729 20.254 1.00 20.66 ATOM 4451 CB ASP B 764 22.73936.046 19.130 1.00 19.31 ATOM 4452 CG ASP B 764 21.474 36.802 18.7671.00 19.31 ATOM 4453 OD1 ASP B 764 20.707 36.320 17.903 1.00 19.87 ATOM4454 OD2 ASP B 764 21.265 37.889 19.341 1.00 17.76 ATOM 4455 C ASP B 76422.862 36.429 21.598 1.00 20.80 ATOM 4456 O ASP B 764 22.021 37.19122.074 1.00 20.53 ATOM 4457 N LEU B 765 23.235 35.319 22.220 1.00 17.19ATOM 4458 CA LEU B 765 22.626 34.934 23.489 1.00 17.73 ATOM 4459 CB LEUB 765 22.337 33.428 23.476 1.00 20.86 ATOM 4460 CG LEU B 765 21.55632.898 22.270 1.00 21.66 ATOM 4461 CD1 LEU B 765 21.264 31.422 22.4441.00 21.03 ATOM 4462 CD2 LEU B 765 20.257 33.679 22.125 1.00 20.47 ATOM4463 C LEU B 765 23.497 35.276 24.697 1.00 18.18 ATOM 4464 O LEU B 76523.205 34.833 25.813 1.00 19.59 ATOM 4465 N SER B 766 24.516 36.11124.475 1.00 19.68 ATOM 4466 CA SER B 766 25.498 36.475 25.504 1.00 20.44ATOM 4467 CB SER B 766 26.478 37.527 24.959 1.00 23.53 ATOM 4468 OG SERB 766 25.937 38.837 24.998 1.00 25.78 ATOM 4469 C SER B 766 24.99736.932 26.872 1.00 20.03 ATOM 4470 O SER B 766 25.695 36.770 27.871 1.0019.65 ATOM 4471 N ALA B 767 23.806 37.513 26.929 1.00 22.57 ATOM 4472 CAALA B 767 23.284 37.974 28.210 1.00 23.91 ATOM 4473 CB ALA B 767 21.94338.682 28.002 1.00 17.04 ATOM 4474 C ALA B 767 23.123 36.832 29.213 1.0023.55 ATOM 4475 O ALA B 767 23.202 37.045 30.426 1.00 24.64 ATOM 4476 NILE B 768 22.911 35.621 28.703 1.00 23.20 ATOM 4477 CA ILE B 768 22.71834.448 29.546 1.00 22.31 ATOM 4478 CB ILE B 768 22.143 33.257 28.7171.00 23.65 ATOM 4479 CG2 ILE B 768 23.253 32.563 27.933 1.00 22.89 ATOM4480 CG1 ILE B 768 21.457 32.255 29.641 1.00 23.26 ATOM 4481 CD1 ILE B768 20.179 32.796 30.272 1.00 23.73 ATOM 4482 C ILE B 768 24.004 33.99930.247 1.00 22.60 ATOM 4483 O ILE B 768 23.958 33.164 31.140 1.00 22.93ATOM 4484 N THR B 769 25.138 34.571 29.849 1.00 21.92 ATOM 4485 CA THR B769 26.438 34.224 30.435 1.00 21.95 ATOM 4486 CB THR B 769 27.525 34.07729.356 1.00 23.33 ATOM 4487 OG1 THR B 769 27.793 35.362 28.778 1.0024.40 ATOM 4488 CG2 THR B 769 27.087 33.111 28.267 1.00 24.02 ATOM 4489C THR B 769 26.962 35.287 31.399 1.00 22.67 ATOM 4490 O THR B 769 27.97335.086 32.073 1.00 22.65 ATOM 4491 N LYS B 770 26.284 36.425 31.452 1.0023.25 ATOM 4492 CA LYS B 770 26.720 37.530 32.296 1.00 23.60 ATOM 4493CB LYS B 770 25.996 38.802 31.849 1.00 21.12 ATOM 4494 CG LYS B 77026.258 39.179 30.403 1.00 20.96 ATOM 4495 CD LYS B 770 27.656 39.75930.206 1.00 20.82 ATOM 4496 CE LYS B 770 27.893 40.115 28.739 1.00 20.75ATOM 4497 NZ LYS B 770 29.176 40.840 28.511 1.00 21.62 ATOM 4498 C LYS B770 26.525 37.339 33.802 1.00 24.02 ATOM 4499 O LYS B 770 25.758 36.47634.239 1.00 23.96 ATOM 4500 N PRO B 771 27.238 38.140 34.618 1.00 24.80ATOM 4501 CD PRO B 771 28.330 39.060 34.249 1.00 25.87 ATOM 4502 CA PROB 771 27.109 38.045 36.076 1.00 25.95 ATOM 4503 CB PRO B 771 27.97639.198 36.569 1.00 25.81 ATOM 4504 CG PRO B 771 29.083 39.215 35.5631.00 26.51 ATOM 4505 C PRO B 771 25.631 38.220 36.440 1.00 26.70 ATOM4506 O PRO B 771 24.905 38.955 35.763 1.00 25.64 ATOM 4507 N TRP B 77225.202 37.546 37.503 1.00 27.13 ATOM 4508 CA TRP B 772 23.811 37.55337.959 1.00 27.52 ATOM 4509 CB TRP B 772 23.744 37.021 39.394 1.00 31.16ATOM 4510 CG TRP B 772 22.355 36.817 39.921 1.00 31.91 ATOM 4511 CD2 TRPB 772 21.272 36.141 39.267 1.00 31.55 ATOM 4512 CE2 TRP B 772 20.17136.166 40.150 1.00 31.84 ATOM 4513 CE3 TRP B 772 21.126 35.516 38.0211.00 31.35 ATOM 4514 CD1 TRP B 772 21.878 37.212 41.138 1.00 31.40 ATOM4515 NE1 TRP B 772 20.569 36.827 41.283 1.00 32.07 ATOM 4516 CZ2 TRP B772 18.937 35.591 39.828 1.00 32.13 ATOM 4517 CZ3 TRP B 772 19.89734.944 37.701 1.00 31.80 ATOM 4518 CH2 TRP B 772 18.819 34.987 38.6021.00 31.93 ATOM 4519 C TRP B 772 23.009 38.853 37.865 1.00 27.06 ATOM4520 O TRP B 772 21.913 38.864 37.305 1.00 27.10 ATOM 4521 N PRO B 77323.533 39.964 38.409 1.00 27.24 ATOM 4522 CD PRO B 773 24.841 40.17639.050 1.00 36.67 ATOM 4523 CA PRO B 773 22.778 41.220 38.336 1.00 26.63ATOM 4524 CB PRO B 773 23.649 42.192 39.133 1.00 36.87 ATOM 4525 CG PROB 773 25.027 41.669 38.902 1.00 37.42 ATOM 4526 C PRO B 773 22.52041.692 36.914 1.00 25.67 ATOM 4527 O PRO B 773 21.476 42.272 36.626 1.0026.52 ATOM 4528 N ILE B 774 23.480 41.443 36.029 1.00 21.82 ATOM 4529 CAILE B 774 23.341 41.834 34.636 1.00 21.26 ATOM 4530 CB ILE B 774 24.70741.788 33.915 1.00 30.27 ATOM 4531 CG2 ILE B 774 24.523 42.062 32.4291.00 30.62 ATOM 4532 CG1 ILE B 774 25.649 42.821 34.543 1.00 31.27 ATOM4533 CD1 ILE B 774 27.075 42.765 34.037 1.00 31.12 ATOM 4534 C ILE B 77422.342 40.909 33.947 1.00 20.74 ATOM 4535 O ILE B 774 21.452 41.37533.239 1.00 21.33 ATOM 4536 N GLN B 775 22.482 39.604 34.166 1.00 22.90ATOM 4537 CA GLN B 775 21.569 38.636 33.565 1.00 23.62 ATOM 4538 CB GLNB 775 21.965 37.205 33.956 1.00 24.73 ATOM 4539 CG GLN B 775 20.80136.214 33.995 1.00 25.27 ATOM 4540 CD GLN B 775 20.070 36.062 32.6611.00 25.01 ATOM 4541 OE1 GLN B 775 18.983 35.495 32.610 1.00 23.97 ATOM4542 NE2 GLN B 775 20.669 36.556 31.583 1.00 25.73 ATOM 4543 C GLN B 77520.127 38.905 33.987 1.00 24.69 ATOM 4544 O GLN B 775 19.213 38.88333.161 1.00 23.74 ATOM 4545 N GLN B 776 19.930 39.158 35.277 1.00 24.42ATOM 4546 CA GLN B 776 18.596 39.440 35.800 1.00 25.46 ATOM 4547 CB GLNB 776 18.647 39.710 37.303 1.00 39.22 ATOM 4548 CG GLN B 776 18.62738.482 38.172 1.00 40.03 ATOM 4549 CD GLN B 776 18.641 38.828 39.6481.00 40.44 ATOM 4550 OE1 GLN B 776 19.635 39.339 40.167 1.00 40.18 ATOM4551 NE2 GLN B 776 17.536 38.554 40.332 1.00 40.01 ATOM 4552 C GLN B 77617.989 40.658 35.121 1.00 24.70 ATOM 4553 O GLN B 776 16.832 40.64134.712 1.00 25.09 ATOM 4554 N ARG B 777 18.773 41.725 35.028 1.00 23.31ATOM 4555 CA ARG B 777 18.298 42.949 34.410 1.00 23.89 ATOM 4556 CB ARGB 777 19.369 44.038 34.481 1.00 27.39 ATOM 4557 CG ARG B 777 18.90245.369 33.917 1.00 27.72 ATOM 4558 CD ARG B 777 19.965 46.434 34.0581.00 28.34 ATOM 4559 NE ARG B 777 21.102 46.209 33.170 1.00 27.57 ATOM4560 CZ ARG B 777 21.029 46.232 31.843 1.00 27.93 ATOM 4561 NH1 ARG B777 19.870 46.468 31.244 1.00 28.38 ATOM 4562 NH2 ARG B 777 22.11946.032 31.113 1.00 27.27 ATOM 4563 C ARG B 777 17.905 42.728 32.958 1.0023.38 ATOM 4564 O ARG B 777 16.814 43.119 32.535 1.00 24.57 ATOM 4565 NILE B 778 18.784 42.089 32.191 1.00 18.64 ATOM 4566 CA ILE B 778 18.48741.853 30.783 1.00 19.91 ATOM 4567 CB ILE B 778 19.729 41.350 30.0281.00 21.48 ATOM 4568 CG2 ILE B 778 19.371 41.065 28.575 1.00 21.88 ATOM4569 CG1 ILE B 778 20.809 42.432 30.077 1.00 22.67 ATOM 4570 CD1 ILE B778 22.127 42.024 29.472 1.00 22.44 ATOM 4571 C ILE B 778 17.333 40.88030.605 1.00 19.30 ATOM 4572 O ILE B 778 16.494 41.063 29.718 1.00 18.16ATOM 4573 N ALA B 779 17.272 39.865 31.459 1.00 20.27 ATOM 4574 CA ALA B779 16.193 38.890 31.393 1.00 21.96 ATOM 4575 CB ALA B 779 16.333 37.88032.513 1.00 23.30 ATOM 4576 C ALA B 779 14.851 39.610 31.495 1.00 21.94ATOM 4577 O ALA B 779 13.896 39.271 30.790 1.00 21.55 ATOM 4578 N GLU B780 14.780 40.615 32.361 1.00 23.66 ATOM 4579 CA GLU B 780 13.539 41.36832.520 1.00 24.79 ATOM 4580 CB GLU B 780 13.643 42.309 33.723 1.00 46.99ATOM 4581 CG GLU B 780 13.971 41.572 35.016 1.00 47.98 ATOM 4582 CD GLUB 780 13.473 42.287 36.255 1.00 48.28 ATOM 4583 OE1 GLU B 780 13.74843.499 36.398 1.00 48.22 ATOM 4584 OE2 GLU B 780 12.814 41.630 37.0891.00 48.29 ATOM 4585 C GLU B 780 13.171 42.144 31.251 1.00 23.73 ATOM4586 O GLU B 780 11.989 42.308 30.931 1.00 23.36 ATOM 4587 N LEU B 78114.180 42.615 30.525 1.00 21.19 ATOM 4588 CA LEU B 781 13.949 43.33629.282 1.00 19.63 ATOM 4589 CB LEU B 781 15.257 43.926 28.761 1.00 24.73ATOM 4590 CG LEU B 781 15.902 44.956 29.687 1.00 25.34 ATOM 4591 CD1 LEUB 781 17.189 45.469 29.065 1.00 25.01 ATOM 4592 CD2 LEU B 781 14.92646.101 29.913 1.00 24.85 ATOM 4593 C LEU B 781 13.393 42.353 28.261 1.0021.36 ATOM 4594 O LEU B 781 12.510 42.686 27.466 1.00 20.39 ATOM 4595 NVAL B 782 13.918 41.134 28.286 1.00 21.98 ATOM 4596 CA VAL B 782 13.45540.112 27.360 1.00 22.60 ATOM 4597 CB VAL B 782 14.275 38.812 27.4991.00 22.53 ATOM 4598 CG1 VAL B 782 13.660 37.713 26.643 1.00 22.91 ATOM4599 CG2 VAL B 782 15.712 39.056 27.054 1.00 23.90 ATOM 4600 C VAL B 78211.988 39.808 27.648 1.00 22.59 ATOM 4601 O VAL B 782 11.159 39.74626.737 1.00 22.68 ATOM 4602 N ALA B 783 11.671 39.628 28.925 1.00 20.36ATOM 4603 CA ALA B 783 10.301 39.327 29.323 1.00 20.69 ATOM 4604 CB ALAB 783 10.232 39.082 30.821 1.00 21.72 ATOM 4605 C ALA B 783 9.376 40.47428.932 1.00 20.76 ATOM 4606 O ALA B 783 8.283 40.249 28.426 1.00 22.62ATOM 4607 N THR B 784 9.823 41.704 29.155 1.00 22.97 ATOM 4608 CA THR B784 9.013 42.862 28.807 1.00 23.28 ATOM 4609 CB THR B 784 9.752 44.18229.139 1.00 23.34 ATOM 4610 OG1 THR B 784 9.934 44.280 30.562 1.00 23.54ATOM 4611 CG2 THR B 784 8.956 45.387 28.645 1.00 23.16 ATOM 4612 C THR B784 8.643 42.846 27.322 1.00 23.86 ATOM 4613 O THR B 784 7.485 43.08626.963 1.00 24.06 ATOM 4614 N GLU B 785 9.612 42.547 26.459 1.00 20.32ATOM 4615 CA GLU B 785 9.333 42.519 25.029 1.00 19.62 ATOM 4616 CB GLU B785 10.633 42.371 24.221 1.00 19.82 ATOM 4617 CG GLU B 785 10.424 42.34622.703 1.00 19.80 ATOM 4618 CD GLU B 785 11.708 42.572 21.908 1.00 22.07ATOM 4619 OE1 GLU B 785 11.800 42.066 20.765 1.00 20.56 ATOM 4620 OE2GLU B 785 12.620 43.264 22.408 1.00 19.00 ATOM 4621 C GLU B 785 8.36041.386 24.709 1.00 20.53 ATOM 4622 O GLU B 785 7.395 41.588 23.964 1.0020.48 ATOM 4623 N PHE B 786 8.603 40.205 25.276 1.00 19.27 ATOM 4624 CAPHE B 786 7.725 39.053 25.054 1.00 20.35 ATOM 4625 CB PHE B 786 8.18537.824 25.853 1.00 27.64 ATOM 4626 CG PHE B 786 9.394 37.122 25.285 1.0028.61 ATOM 4627 CD1 PHE B 786 9.799 37.330 23.971 1.00 28.46 ATOM 4628CD2 PHE B 786 10.111 36.225 26.072 1.00 28.06 ATOM 4629 CE1 PHE B 78610.903 36.652 23.451 1.00 28.92 ATOM 4630 CE2 PHE B 786 11.212 35.54325.561 1.00 28.43 ATOM 4631 CZ PHE B 786 11.608 35.758 24.250 1.00 28.30ATOM 4632 C PHE B 786 6.289 39.380 25.475 1.00 20.75 ATOM 4633 O PHE B786 5.340 39.061 24.760 1.00 18.68 ATOM 4634 N PHE B 787 6.144 40.00326.646 1.00 22.35 ATOM 4635 CA PHE B 787 4.825 40.361 27.160 1.00 21.89ATOM 4636 CB PHE B 787 4.917 40.801 28.632 1.00 21.52 ATOM 4637 CG PHE B787 5.419 39.729 29.567 1.00 22.41 ATOM 4638 CD1 PHE B 787 5.256 38.37629.265 1.00 22.32 ATOM 4639 CD2 PHE B 787 6.035 40.070 30.771 1.00 21.61ATOM 4640 CE1 PHE B 787 5.698 37.384 30.148 1.00 22.73 ATOM 4641 CE2 PHEB 787 6.478 39.085 31.653 1.00 22.56 ATOM 4642 CZ PHE B 787 6.309 37.74231.341 1.00 21.88 ATOM 4643 C PHE B 787 4.154 41.453 26.317 1.00 21.60ATOM 4644 O PHE B 787 2.924 41.484 26.195 1.00 21.58 ATOM 4645 N ASP B788 4.950 42.338 25.721 1.00 20.66 ATOM 4646 CA ASP B 788 4.387 43.38424.872 1.00 21.38 ATOM 4647 CB ASP B 788 5.459 44.404 24.467 1.00 29.62ATOM 4648 CG ASP B 788 4.892 45.559 23.646 1.00 31.03 ATOM 4649 OD1 ASPB 788 4.010 46.284 24.159 1.00 31.00 ATOM 4650 OD2 ASP B 788 5.32745.750 22.486 1.00 30.30 ATOM 4651 C ASP B 788 3.802 42.712 23.630 1.0021.98 ATOM 4652 O ASP B 788 2.754 43.116 23.138 1.00 20.90 ATOM 4653 NGLN B 789 4.480 41.686 23.117 1.00 18.78 ATOM 4654 CA GLN B 789 3.95040.980 21.958 1.00 19.35 ATOM 4655 CB GLN B 789 4.947 39.965 21.397 1.0018.41 ATOM 4656 CG GLN B 789 4.283 39.057 20.363 1.00 19.65 ATOM 4657 CDGLN B 789 5.228 38.067 19.715 1.00 19.91 ATOM 4658 OE1 GLN B 789 4.80537.004 19.253 1.00 20.58 ATOM 4659 NE2 GLN B 789 6.503 38.413 19.6631.00 17.85 ATOM 4660 C GLN B 789 2.690 40.240 22.382 1.00 19.10 ATOM4661 O GLN B 789 1.728 40.154 21.622 1.00 19.13 ATOM 4662 N GLY B 7902.713 39.701 23.598 1.00 20.13 ATOM 4663 CA GLY B 790 1.565 38.98324.118 1.00 21.62 ATOM 4664 C GLY B 790 0.338 39.870 24.089 1.00 21.39ATOM 4665 O GLY B 790 −0.748 39.426 23.711 1.00 20.51 ATOM 4666 N ASP B791 0.506 41.127 24.491 1.00 21.64 ATOM 4667 CA ASP B 791 −0.612 42.06624.488 1.00 23.10 ATOM 4668 CB ASP B 791 −0.205 43.401 25.128 1.00 27.91ATOM 4669 CG ASP B 791 0.161 43.263 26.599 1.00 28.04 ATOM 4670 OD1 ASPB 791 −0.368 42.352 27.271 1.00 28.51 ATOM 4671 OD2 ASP B 791 0.96744.083 27.092 1.00 29.30 ATOM 4672 C ASP B 791 −1.118 42.307 23.061 1.0022.57 ATOM 4673 O ASP B 791 −2.328 42.422 22.837 1.00 22.71 ATOM 4674 NARG B 792 −0.196 42.388 22.103 1.00 22.55 ATOM 4675 CA ARG B 792 −0.55742.600 20.701 1.00 21.86 ATOM 4676 CB ARG B 792 0.697 42.794 19.831 1.0025.58 ATOM 4677 CG ARG B 792 1.559 44.015 20.155 1.00 26.82 ATOM 4678 CDARG B 792 1.268 45.192 19.225 1.00 27.03 ATOM 4679 NE ARG B 792 1.60244.929 17.819 1.00 26.18 ATOM 4680 CZ ARG B 792 2.768 45.220 17.247 1.0026.00 ATOM 4681 NH1 ARG B 792 3.746 45.785 17.950 1.00 26.11 ATOM 4682NH2 ARG B 792 2.943 44.982 15.954 1.00 27.12 ATOM 4683 C ARG B 792−1.338 41.393 20.179 1.00 21.59 ATOM 4684 O ARG B 792 −2.251 41.54119.366 1.00 22.04 ATOM 4685 N GLU B 793 −0.981 40.199 20.640 1.00 21.27ATOM 4686 CA GLU B 793 −1.678 38.999 20.189 1.00 23.41 ATOM 4687 CB GLUB 793 −0.915 37.741 20.613 1.00 32.13 ATOM 4688 CG GLU B 793 0.52337.716 20.126 1.00 32.18 ATOM 4689 CD GLU B 793 1.199 36.378 20.354 1.0032.76 ATOM 4690 OE1 GLU B 793 0.883 35.713 21.363 1.00 33.25 ATOM 4691OE2 GLU B 793 2.058 35.998 19.531 1.00 32.81 ATOM 4692 C GLU B 793−3.106 38.946 20.726 1.00 23.75 ATOM 4693 O GLU B 793 −4.044 38.61019.995 1.00 22.66 ATOM 4694 N ARG B 794 −3.277 39.283 21.999 1.00 24.04ATOM 4695 CA ARG B 794 −4.603 39.256 22.599 1.00 24.34 ATOM 4696 CB ARGB 794 −4.564 39.780 24.038 1.00 32.14 ATOM 4697 CG ARG B 794 −3.33239.401 24.824 1.00 33.26 ATOM 4698 CD ARG B 794 −3.543 39.603 26.3161.00 33.20 ATOM 4699 NE ARG B 794 −4.342 38.518 26.866 1.00 33.66 ATOM4700 CZ ARG B 794 −3.964 37.749 27.881 1.00 33.17 ATOM 4701 NH1 ARG B794 −2.794 37.948 28.472 1.00 33.10 ATOM 4702 NH2 ARG B 794 −4.74836.759 28.285 1.00 33.54 ATOM 4703 C ARG B 794 −5.566 40.119 21.797 1.0025.06 ATOM 4704 O ARG B 794 −6.713 39.740 21.563 1.00 24.85 ATOM 4705 NLYS B 795 −5.090 41.279 21.369 1.00 26.49 ATOM 4706 CA LYS B 795 −5.92842.205 20.627 1.00 27.67 ATOM 4707 CB LYS B 795 −5.412 43.633 20.8211.00 43.32 ATOM 4708 CG LYS B 795 −5.021 43.940 22.260 1.00 43.98 ATOM4709 CD LYS B 795 −4.846 45.433 22.504 1.00 44.35 ATOM 4710 CE LYS B 795−6.121 46.059 23.052 1.00 44.46 ATOM 4711 NZ LYS B 795 −7.293 45.85522.159 1.00 44.56 ATOM 4712 C LYS B 795 −6.032 41.883 19.140 1.00 27.05ATOM 4713 O LYS B 795 −7.125 41.624 18.636 1.00 28.54 ATOM 4714 N GLU B796 −4.894 41.885 18.451 1.00 25.18 ATOM 4715 CA GLU B 796 −4.842 41.63417.007 1.00 24.55 ATOM 4716 CB GLU B 796 −3.464 42.009 16.464 1.00 28.07ATOM 4717 CG GLU B 796 −2.991 43.391 16.889 1.00 29.00 ATOM 4718 CD GLUB 796 −1.615 43.741 16.348 1.00 28.65 ATOM 4719 OE1 GLU B 796 −0.96244.626 16.931 1.00 29.39 ATOM 4720 OE2 GLU B 796 −1.187 43.144 15.3401.00 29.53 ATOM 4721 C GLU B 796 −5.173 40.214 16.549 1.00 24.25 ATOM4722 O GLU B 796 −5.637 40.011 15.423 1.00 25.17 ATOM 4723 N LEU B 797−4.922 39.228 17.399 1.00 22.33 ATOM 4724 CA LEU B 797 −5.201 37.84717.021 1.00 21.19 ATOM 4725 CB LEU B 797 −3.923 36.999 17.111 1.00 24.95ATOM 4726 CG LEU B 797 −2.757 37.369 16.184 1.00 24.74 ATOM 4727 CD1 LEUB 797 −1.555 36.486 16.498 1.00 24.36 ATOM 4728 CD2 LEU B 797 −3.17337.209 14.720 1.00 25.36 ATOM 4729 C LEU B 797 −6.295 37.239 17.889 1.0022.61 ATOM 4730 O LEU B 797 −6.717 36.108 17.657 1.00 21.44 ATOM 4731 NASN B 798 −6.756 38.002 18.877 1.00 22.45 ATOM 4732 CA ASN B 798 −7.80737.556 19.791 1.00 23.65 ATOM 4733 CB ASN B 798 −9.165 37.569 19.0891.00 32.89 ATOM 4734 CG ASN B 798 −10.163 38.479 19.777 1.00 34.23 ATOM4735 OD1 ASN B 798 −10.392 38.372 20.982 1.00 32.44 ATOM 4736 ND2 ASN B798 −10.767 39.381 19.010 1.00 35.38 ATOM 4737 C ASN B 798 −7.532 36.16420.352 1.00 23.21 ATOM 4738 O ASN B 798 −8.414 35.305 20.384 1.00 23.77ATOM 4739 N ILE B 799 −6.299 35.945 20.794 1.00 22.30 ATOM 4740 CA ILE B799 −5.914 34.655 21.359 1.00 24.01 ATOM 4741 CB ILE B 799 −4.993 33.86820.403 1.00 37.22 ATOM 4742 CG2 ILE B 799 −5.661 33.695 19.047 1.0037.98 ATOM 4743 CG1 ILE B 799 −3.664 34.613 20.244 1.00 37.41 ATOM 4744CD1 ILE B 799 −2.556 33.780 19.633 1.00 37.91 ATOM 4745 C ILE B 799−5.146 34.867 22.658 1.00 23.86 ATOM 4746 O ILE B 799 −4.542 35.92222.867 1.00 22.69 ATOM 4747 N GLU B 800 −5.178 33.870 23.533 1.00 27.63ATOM 4748 CA GLU B 800 −4.442 33.961 24.787 1.00 28.49 ATOM 4749 CB GLUB 800 −4.912 32.882 25.766 1.00 54.96 ATOM 4750 CG GLU B 800 −4.15932.874 27.091 1.00 55.87 ATOM 4751 CD GLU B 800 −4.612 31.758 28.0181.00 56.25 ATOM 4752 OE1 GLU B 800 −4.037 31.633 29.121 1.00 56.19 ATOM4753 OE2 GLU B 800 −5.541 31.008 27.645 1.00 56.33 ATOM 4754 C GLU B 800−2.995 33.711 24.385 1.00 28.05 ATOM 4755 O GLU B 800 −2.712 32.79123.616 1.00 28.04 ATOM 4756 N PRO B 801 −2.060 34.539 24.866 1.00 26.29ATOM 4757 CD PRO B 801 −2.159 35.766 25.673 1.00 32.02 ATOM 4758 CA PROB 801 −0.675 34.280 24.465 1.00 25.59 ATOM 4759 CB PRO B 801 0.04735.561 24.875 1.00 32.25 ATOM 4760 CG PRO B 801 −0.719 35.993 26.0851.00 32.69 ATOM 4761 C PRO B 801 −0.115 33.044 25.155 1.00 25.64 ATOM4762 O PRO B 801 −0.688 32.552 26.127 1.00 26.27 ATOM 4763 N THR B 8020.990 32.529 24.634 1.00 27.06 ATOM 4764 CA THR B 802 1.622 31.36625.242 1.00 27.00 ATOM 4765 CB THR B 802 2.731 30.798 24.340 1.00 41.37ATOM 4766 OG1 TER B 802 3.289 29.626 24.947 1.00 42.49 ATOM 4767 CG2 THRB 802 3.824 31.831 24.124 1.00 41.44 ATOM 4768 C THR B 802 2.220 31.83926.562 1.00 26.88 ATOM 4769 O THR B 802 2.390 33.041 26.776 1.00 25.80ATOM 4770 N ASP B 803 2.526 30.902 27.449 1.00 25.95 ATOM 4771 CA ASP B803 3.096 31.248 28.744 1.00 25.37 ATOM 4772 CB ASP B 803 3.534 29.97429.469 1.00 34.61 ATOM 4773 CG ASP B 803 2.374 29.260 30.141 1.00 34.77ATOM 4774 OD1 ASP B 803 1.263 29.252 29.568 1.00 34.79 ATOM 4775 OD2 ASPB 803 2.581 28.699 31.238 1.00 35.35 ATOM 4776 C ASP B 803 4.260 32.24028.673 1.00 24.64 ATOM 4777 O ASP B 803 4.283 33.226 29.409 1.00 25.72ATOM 4778 N LEU B 804 5.217 31.999 27.785 1.00 27.10 ATOM 4779 CA LEU B804 6.359 32.899 27.686 1.00 26.94 ATOM 4780 CB LEU B 804 7.423 32.30026.757 1.00 52.26 ATOM 4781 CG LEU B 804 7.015 31.757 25.390 1.00 53.10ATOM 4782 CD1 LEU B 804 7.196 32.830 24.331 1.00 53.31 ATOM 4783 CD2 LEUB 804 7.882 30.551 25.052 1.00 53.28 ATOM 4784 C LEU B 804 6.012 34.32927.268 1.00 26.18 ATOM 4785 O LEU B 804 6.806 35.240 27.474 1.00 26.67ATOM 4786 N MET B 805 4.823 34.537 26.705 1.00 24.63 ATOM 4787 CA MET B805 4.423 35.880 26.285 1.00 24.58 ATOM 4788 CB MET B 805 4.151 35.90224.780 1.00 30.72 ATOM 4789 CG MET B 805 5.333 35.419 23.963 1.00 31.20ATOM 4790 SD MET B 805 5.137 35.642 22.209 1.00 31.94 ATOM 4791 CE MET B805 6.846 35.924 21.734 1.00 31.24 ATOM 4792 C MET B 805 3.191 36.37327.044 1.00 23.91 ATOM 4793 O MET B 805 2.552 37.352 26.647 1.00 23.70ATOM 4794 N ASN B 806 2.884 35.699 28.147 1.00 22.71 ATOM 4795 CA ASN B806 1.728 36.042 28.970 1.00 23.25 ATOM 4796 CB ASN B 806 0.917 34.77229.255 1.00 28.25 ATOM 4797 CG ASN B 806 −0.352 35.045 30.054 1.00 27.90ATOM 4798 OD1 ASN B 806 −0.642 36.181 30.420 1.00 28.09 ATOM 4799 ND2ASN B 806 −1.114 33.991 30.325 1.00 28.50 ATOM 4800 C ASN B 806 2.17736.683 30.281 1.00 23.54 ATOM 4801 O ASN B 806 2.651 35.992 31.178 1.0024.88 ATOM 4802 N ARG B 807 2.023 38.003 30.386 1.00 22.01 ATOM 4803 CAARG B 807 2.417 38.748 31.585 1.00 22.16 ATOM 4804 CB ARG B 807 2.04040.223 31.426 1.00 30.21 ATOM 4805 CG ARG B 807 2.729 41.167 32.399 1.0030.83 ATOM 4806 CD ARG B 807 2.164 42.572 32.270 1.00 30.96 ATOM 4807 NEARG B 807 2.118 43.013 30.879 1.00 31.52 ATOM 4808 CZ ARG B 807 3.16143.482 30.205 1.00 31.30 ATOM 4809 NH1 ARG B 807 4.347 43.583 30.7951.00 31.76 ATOM 4810 NH2 ARG B 807 3.019 43.843 28.935 1.00 30.41 ATOM4811 C ARG B 807 1.753 38.186 32.844 1.00 23.50 ATOM 4812 O ARG B 8072.324 38.241 33.933 1.00 22.48 ATOM 4813 N GLU B 808 0.549 37.645 32.6941.00 27.30 ATOM 4814 CA GLU B 808 −0.164 37.075 33.833 1.00 27.61 ATOM4815 CB GLU B 808 −1.585 36.680 33.421 1.00 44.18 ATOM 4816 CG GLU B 808−2.572 37.835 33.427 1.00 44.75 ATOM 4817 CD GLU B 808 −3.887 37.49432.750 1.00 45.10 ATOM 4818 OE1 GLU B 808 −4.418 36.388 32.990 1.0044.66 ATOM 4819 OE2 GLU B 808 −4.390 38.342 31.982 1.00 44.84 ATOM 4820C GLU B 808 0.559 35.865 34.416 1.00 28.07 ATOM 4821 O GLU B 808 0.42635.572 35.604 1.00 27.52 ATOM 4822 N LYS B 809 1.328 35.171 33.582 1.0030.73 ATOM 4823 CA LYS B 809 2.063 33.984 34.015 1.00 31.34 ATOM 4824 CBLYS B 809 1.888 32.856 32.988 1.00 44.52 ATOM 4825 CG LYS B 809 0.44332.434 32.739 1.00 44.86 ATOM 4826 CD LYS B 809 −0.095 31.554 33.8531.00 45.24 ATOM 4827 CE LYS B 809 0.499 30.152 33.794 1.00 45.08 ATOM4828 NZ LYS B 809 0.023 29.386 32.607 1.00 45.32 ATOM 4829 C LYS B 8093.549 34.280 34.187 1.00 31.41 ATOM 4830 O LYS B 809 4.389 33.396 34.0141.00 31.64 ATOM 4831 N LYS B 810 3.874 35.522 34.534 1.00 29.88 ATOM4832 CA LYS B 810 5.266 35.924 34.714 1.00 29.67 ATOM 4833 CB LYS B 8105.350 37.417 35.033 1.00 35.65 ATOM 4834 CG LYS B 810 4.772 37.78736.384 1.00 35.72 ATOM 4835 CD LYS B 810 4.977 39.256 36.681 1.00 36.06ATOM 4836 CE LYS B 810 4.445 39.617 38.058 1.00 36.21 ATOM 4837 NZ LYS B810 4.806 41.010 38.416 1.00 36.50 ATOM 4838 C LYS B 810 5.981 35.13535.815 1.00 29.55 ATOM 4839 O LYS B 810 7.204 35.220 35.954 1.00 29.80ATOM 4840 N ASN B 811 5.221 34.371 36.595 1.00 28.77 ATOM 4841 CA ASN B811 5.809 33.576 37.672 1.00 28.26 ATOM 4842 CB ASN B 811 4.716 33.11338.643 1.00 33.98 ATOM 4843 CG ASN B 811 3.760 32.122 38.012 1.00 33.96ATOM 4844 OD1 ASN B 811 4.059 30.935 37.904 1.00 34.26 ATOM 4845 ND2 ASNB 811 2.607 32.611 37.578 1.00 34.21 ATOM 4846 C ASN B 811 6.558 32.36437.122 1.00 28.78 ATOM 4847 O ASN B 811 7.277 31.681 37.852 1.00 28.05ATOM 4848 N LYS B 812 6.391 32.112 35.826 1.00 27.42 ATOM 4849 CA LYS B812 7.034 30.983 35.161 1.00 27.06 ATOM 4850 CB LYS B 812 6.175 30.51833.980 1.00 41.02 ATOM 4851 CG LYS B 812 5.384 29.246 34.224 1.00 41.61ATOM 4852 CD LYS B 812 4.485 29.360 35.436 1.00 41.66 ATOM 4853 CE LYS B812 3.735 28.062 35.681 1.00 41.87 ATOM 4854 NZ LYS B 812 4.665 26.92135.913 1.00 41.60 ATOM 4855 C LYS B 812 8.436 31.306 34.655 1.00 25.94ATOM 4856 O LYS B 812 9.169 30.409 34.248 1.00 27.20 ATOM 4857 N ILE B813 8.814 32.579 34.693 1.00 24.47 ATOM 4858 CA ILE B 813 10.126 32.99334.203 1.00 24.87 ATOM 4859 CB ILE B 813 10.353 34.509 34.452 1.00 27.03ATOM 4860 CG2 ILE B 813 11.812 34.887 34.190 1.00 26.32 ATOM 4861 CG1ILE B 813 9.420 35.312 33.537 1.00 27.43 ATOM 4862 CD1 ILE B 813 9.42236.809 33.792 1.00 27.47 ATOM 4863 C ILE B 813 11.321 32.198 34.725 1.0024.94 ATOM 4864 O ILE B 813 12.153 31.747 33.940 1.00 24.37 ATOM 4865 NPRO B 814 11.433 32.015 36.051 1.00 23.33 ATOM 4866 CD PRO B 814 10.64932.549 37.180 1.00 25.56 ATOM 4867 CA PRO B 814 12.588 31.251 36.5361.00 24.96 ATOM 4868 CB PRO B 814 12.336 31.171 38.041 1.00 25.58 ATOM4869 CG PRO B 814 11.650 32.478 38.317 1.00 25.37 ATOM 4870 C PRO B 81412.708 29.870 35.892 1.00 24.30 ATOM 4871 O PRO B 814 13.752 29.51935.346 1.00 26.00 ATOM 4872 N SER B 815 11.629 29.101 35.942 1.00 27.38ATOM 4873 CA SER B 815 11.631 27.759 35.372 1.00 28.28 ATOM 4874 CB SERB 815 10.320 27.048 35.705 1.00 30.12 ATOM 4875 OG SER B 815 9.21427.762 35.193 1.00 30.40 ATOM 4876 C SER B 815 11.852 27.767 33.860 1.0028.08 ATOM 4877 O SER B 815 12.426 26.831 33.307 1.00 28.51 ATOM 4878 NMET B 816 11.405 28.822 33.190 1.00 26.53 ATOM 4879 CA MET B 816 11.58128.899 31.743 1.00 25.98 ATOM 4880 CB MET B 816 10.633 29.940 31.1471.00 38.18 ATOM 4881 CG MET B 816 9.173 29.635 31.422 1.00 38.60 ATOM4882 SD MET B 816 8.038 30.687 30.502 1.00 40.03 ATOM 4883 CE MET B 8168.543 32.319 31.070 1.00 38.78 ATOM 4884 C MET B 816 13.021 29.22431.384 1.00 25.44 ATOM 4885 O MET B 816 13.540 28.736 30.383 1.00 25.22ATOM 4886 N GLN B 817 13.666 30.047 32.207 1.00 24.56 ATOM 4887 CA GLN B817 15.057 30.413 31.984 1.00 24.03 ATOM 4888 CB GLN B 817 15.503 31.46533.000 1.00 23.33 ATOM 4889 CG GLN B 817 15.074 32.885 32.672 1.00 23.25ATOM 4890 CD GLN B 817 15.603 33.349 31.331 1.00 24.23 ATOM 4891 OE1 GLNB 817 15.073 32.980 30.285 1.00 23.44 ATOM 4892 NE2 GLN B 817 16.66634.146 31.354 1.00 23.50 ATOM 4893 C GLN B 817 15.923 29.166 32.122 1.0024.21 ATOM 4894 O GLN B 817 16.862 28.961 31.350 1.00 25.39 ATOM 4895 NVAL B 818 15.609 28.342 33.116 1.00 22.52 ATOM 4896 CA VAL B 818 16.35027.103 33.331 1.00 24.31 ATOM 4897 CB VAL B 818 15.820 26.335 34.5621.00 26.47 ATOM 4898 CG1 VAL B 818 16.541 24.993 34.688 1.00 26.36 ATOM4899 CG2 VAL B 818 16.037 27.164 35.815 1.00 26.36 ATOM 4900 C VAL B 81816.182 26.236 32.085 1.00 23.82 ATOM 4901 O VAL B 818 17.148 25.65931.588 1.00 23.44 ATOM 4902 N GLY B 819 14.953 26.172 31.577 1.00 26.53ATOM 4903 CA GLY B 819 14.669 25.386 30.385 1.00 25.97 ATOM 4904 C GLY B819 15.410 25.903 29.164 1.00 25.98 ATOM 4905 O GLY B 819 15.928 25.12828.365 1.00 25.51 ATOM 4906 N PHE B 820 15.455 27.223 29.021 1.00 22.89ATOM 4907 CA PHE B 820 16.149 27.869 27.906 1.00 22.59 ATOM 4908 CB PHEB 820 15.941 29.389 27.997 1.00 24.78 ATOM 4909 CG PHE B 820 16.82130.195 27.078 1.00 26.25 ATOM 4910 CD1 PHE B 820 16.716 30.071 25.6961.00 25.90 ATOM 4911 CD2 PHE B 820 17.742 31.104 27.601 1.00 24.43 ATOM4912 CE1 PHE B 820 17.513 30.841 24.845 1.00 25.64 ATOM 4913 CE2 PHE B820 18.545 31.877 26.762 1.00 25.89 ATOM 4914 CZ PHE B 820 18.432 31.74725.381 1.00 25.35 ATOM 4915 C PHE B 820 17.641 27.535 27.953 1.00 22.74ATOM 4916 O PHE B 820 18.256 27.231 26.932 1.00 21.86 ATOM 4917 N ILE B821 18.222 27.595 29.143 1.00 24.60 ATOM 4918 CA ILE B 821 19.640 27.30329.295 1.00 26.01 ATOM 4919 CB ILE B 821 20.099 27.593 30.739 1.00 23.25ATOM 4920 CG2 ILE B 821 21.480 27.001 30.984 1.00 23.21 ATOM 4921 CG1ILE B 821 20.096 29.105 30.980 1.00 22.99 ATOM 4922 CD1 ILE B 821 20.40929.506 32.410 1.00 23.26 ATOM 4923 C ILE B 821 19.944 25.848 28.929 1.0026.27 ATOM 4924 O ILE B 821 20.893 25.565 28.187 1.00 26.66 ATOM 4925 NASP B 822 19.129 24.931 29.436 1.00 29.94 ATOM 4926 CA ASP B 822 19.33223.511 29.168 1.00 30.98 ATOM 4927 CB ASP B 822 18.391 22.657 30.0231.00 31.31 ATOM 4928 CG ASP B 822 18.798 22.617 31.478 1.00 31.53 ATOM4929 OD1 ASP B 822 19.984 22.882 31.771 1.00 31.53 ATOM 4930 OD2 ASP B822 17.939 22.301 32.330 1.00 31.44 ATOM 4931 C ASP B 822 19.147 23.10327.715 1.00 30.90 ATOM 4932 O ASP B 822 19.963 22.368 27.162 1.00 31.36ATOM 4933 N ALA B 823 18.070 23.577 27.102 1.00 28.23 ATOM 4934 CA ALA B823 17.757 23.217 25.724 1.00 27.21 ATOM 4935 CB ALA B 823 16.268 23.43825.470 1.00 28.57 ATOM 4936 C ALA B 823 18.563 23.923 24.642 1.00 27.07ATOM 4937 O ALA B 823 18.861 23.330 23.607 1.00 27.74 ATOM 4938 N ILE B824 18.926 25.178 24.878 1.00 23.52 ATOM 4939 CA ILE B 824 19.639 25.95023.869 1.00 23.73 ATOM 4940 CB ILE B 824 18.802 27.205 23.482 1.00 34.66ATOM 4941 CG2 ILE B 824 19.646 28.198 22.686 1.00 35.04 ATOM 4942 CG1ILE B 824 17.571 26.780 22.682 1.00 35.26 ATOM 4943 CD1 ILE B 824 17.91226.136 21.354 1.00 35.75 ATOM 4944 C ILE B 824 21.052 26.416 24.195 1.0023.62 ATOM 4945 O ILE B 824 21.963 26.256 23.387 1.00 24.76 ATOM 4946 NCYS B 825 21.242 26.982 25.381 1.00 25.35 ATOM 4947 CA CYS B 825 22.53727.545 25.750 1.00 25.12 ATOM 4948 CB CYS B 825 22.322 28.602 26.8271.00 22.81 ATOM 4949 SG CYS B 825 21.059 29.783 26.356 1.00 22.83 ATOM4950 C CYS B 825 23.700 26.653 26.169 1.00 25.45 ATOM 4951 O CYS B 82524.796 26.778 25.627 1.00 26.37 ATOM 4952 N LEU B 826 23.477 25.78327.145 1.00 25.06 ATOM 4953 CA LEU B 826 24.541 24.921 27.651 1.00 26.86ATOM 4954 CB LEU B 826 23.954 23.898 28.626 1.00 41.13 ATOM 4955 CG LEUB 826 24.523 23.958 30.048 1.00 41.95 ATOM 4956 CD1 LEU B 826 24.53725.392 30.550 1.00 41.82 ATOM 4957 CD2 LEU B 826 23.695 23.076 30.9671.00 41.66 ATOM 4958 C LEU B 826 25.397 24.208 26.606 1.00 25.29 ATOM4959 O LEU B 826 26.623 24.327 26.619 1.00 27.23 ATOM 4960 N GLN B 82724.764 23.467 25.703 1.00 27.86 ATOM 4961 CA GLN B 827 25.512 22.73724.679 1.00 27.22 ATOM 4962 CB GLN B 827 24.560 21.935 23.796 1.00 43.35ATOM 4963 CG GLN B 827 23.663 20.981 24.546 1.00 43.82 ATOM 4964 CD GLNB 827 22.683 20.289 23.626 1.00 44.18 ATOM 4965 OE1 GLN B 827 23.07719.509 22.759 1.00 44.12 ATOM 4966 NE2 GLN B 827 21.396 20.582 23.8001.00 44.14 ATOM 4967 C GLN B 827 26.346 23.652 23.791 1.00 27.96 ATOM4968 O GLN B 827 27.469 23.310 23.417 1.00 27.98 ATOM 4969 N LEU B 82825.789 24.807 23.439 1.00 23.58 ATOM 4970 CA LEU B 828 26.491 25.75322.585 1.00 23.82 ATOM 4971 CB LEU B 828 25.574 26.922 22.212 1.00 24.08ATOM 4972 CG LEU B 828 26.222 28.012 21.353 1.00 24.69 ATOM 4973 CD1 LEUB 828 26.835 27.406 20.087 1.00 24.52 ATOM 4974 CD2 LEU B 828 25.18029.058 21.001 1.00 24.55 ATOM 4975 C LEU B 828 27.768 26.289 23.218 1.0023.20 ATOM 4976 O LEU B 828 28.824 26.307 22.586 1.00 23.94 ATOM 4977 NTYR B 829 27.681 26.736 24.464 1.00 24.32 ATOM 4978 CA TYR B 829 28.86627.266 25.122 1.00 24.21 ATOM 4979 CB TYR B 829 28.461 28.040 26.3781.00 23.28 ATOM 4980 CG TYR B 829 27.724 29.315 26.015 1.00 21.35 ATOM4981 CD1 TYR B 829 28.358 30.318 25.280 1.00 22.17 ATOM 4982 CE1 TYR B829 27.673 31.462 24.866 1.00 21.77 ATOM 4983 CD2 TYR B 829 26.38329.488 26.337 1.00 23.05 ATOM 4984 CE2 TYR B 829 25.686 30.630 25.9281.00 21.86 ATOM 4985 CZ TYR B 829 26.338 31.609 25.192 1.00 22.76 ATOM4986 OH TYR B 829 25.662 32.733 24.759 1.00 20.79 ATOM 4987 C TYR B 82929.871 26.163 25.428 1.00 25.08 ATOM 4988 O TYR B 829 31.076 26.40825.465 1.00 24.92 ATOM 4989 N GLU B 830 29.380 24.944 25.628 1.00 25.46ATOM 4990 CA GLU B 830 30.278 23.826 25.892 1.00 27.34 ATOM 4991 CB GLUB 830 29.482 22.572 26.268 1.00 35.78 ATOM 4992 CG GLU B 830 28.82222.637 27.635 1.00 36.70 ATOM 4993 CD GLU B 830 27.981 21.409 27.9381.00 36.51 ATOM 4994 OE1 GLU B 830 27.433 21.318 29.056 1.00 36.91 ATOM4995 OE2 GLU B 830 27.863 20.533 27.053 1.00 37.38 ATOM 4996 C GLU B 83031.087 23.563 24.624 1.00 26.06 ATOM 4997 O GLU B 830 32.305 23.37724.679 1.00 26.54 ATOM 4998 N ALA B 831 30.398 23.566 23.486 1.00 25.64ATOM 4999 CA ALA B 831 31.026 23.332 22.189 1.00 23.78 ATOM 5000 CB ALAB 831 29.952 23.253 21.093 1.00 30.54 ATOM 5001 C ALA B 831 32.03124.427 21.853 1.00 24.89 ATOM 5002 O ALA B 831 33.110 24.151 21.328 1.0024.70 ATOM 5003 N LEU B 832 31.679 25.671 22.158 1.00 22.52 ATOM 5004 CALEU B 832 32.578 26.778 21.872 1.00 23.49 ATOM 5005 CB LEU B 832 31.90528.116 22.198 1.00 21.26 ATOM 5006 CG LEU B 832 32.754 29.333 21.8241.00 22.68 ATOM 5007 CD1 LEU B 832 33.199 29.213 20.369 1.00 21.78 ATOM5008 CD2 LEU B 832 31.963 30.613 22.042 1.00 22.23 ATOM 5009 C LEU B 83233.854 26.627 22.694 1.00 22.63 ATOM 5010 O LEU B 832 34.955 26.91622.220 1.00 23.62 ATOM 5011 N THR B 833 33.697 26.165 23.928 1.00 26.15ATOM 5012 CA THR B 833 34.828 25.973 24.822 1.00 27.69 ATOM 5013 CB THRB 833 34.350 25.621 26.247 1.00 25.51 ATOM 5014 OG1 THR B 833 33.54926.695 26.759 1.00 27.15 ATOM 5015 CG2 THR B 833 35.539 25.401 27.1811.00 26.42 ATOM 5016 C THR B 833 35.733 24.862 24.293 1.00 27.86 ATOM5017 O THR B 833 36.949 24.876 24.506 1.00 27.78 ATOM 5018 N HIS B 83435.132 23.904 23.600 1.00 29.42 ATOM 5019 CA HIS B 834 35.885 22.79523.026 1.00 30.11 ATOM 5020 CB HIS B 834 34.920 21.755 22.449 1.00 46.85ATOM 5021 CG HIS B 834 35.571 20.457 22.084 1.00 47.63 ATOM 5022 CD2 HISB 834 36.207 20.064 20.955 1.00 47.79 ATOM 5023 ND1 HIS B 834 35.62119.382 22.945 1.00 47.75 ATOM 5024 CE1 HIS B 834 36.257 18.381 22.3611.00 47.72 ATOM 5025 NE2 HIS B 834 36.623 18.769 21.153 1.00 47.50 ATOM5026 C HIS B 834 36.773 23.351 21.912 1.00 30.08 ATOM 5027 O HIS B 83437.939 22.972 21.773 1.00 30.93 ATOM 5028 N VAL B 835 36.209 24.25921.119 1.00 25.19 ATOM 5029 CA VAL B 835 36.935 24.866 20.015 1.00 25.37ATOM 5030 CB VAL B 835 35.986 25.730 19.144 1.00 27.06 ATOM 5031 CG1 VALB 835 36.764 26.460 18.071 1.00 27.88 ATOM 5032 CG2 VAL B 835 34.93224.842 18.505 1.00 27.32 ATOM 5033 C VAL B 835 38.107 25.704 20.515 1.0025.36 ATOM 5034 O VAL B 835 39.204 25.626 19.971 1.00 25.68 ATOM 5035 NSER B 836 37.874 26.504 21.552 1.00 28.63 ATOM 5036 CA SER B 836 38.92627.340 22.130 1.00 29.30 ATOM 5037 CB SER B 836 38.924 28.734 21.4891.00 32.06 ATOM 5038 OG SER B 836 39.982 29.529 21.996 1.00 32.73 ATOM5039 C SER B 836 38.674 27.454 23.629 1.00 29.51 ATOM 5040 O SER B 83637.718 28.096 24.058 1.00 28.84 ATOM 5041 N GLU B 837 39.530 26.82524.426 1.00 26.81 ATOM 5042 CA GLU B 837 39.359 26.846 25.874 1.00 27.10ATOM 5043 CB GLU B 837 40.430 25.972 26.536 1.00 50.60 ATOM 5044 CG GLUB 837 41.843 26.245 26.062 1.00 51.48 ATOM 5045 CD GLU B 837 42.81125.145 26.460 1.00 51.89 ATOM 5046 OE1 GLU B 837 42.985 24.912 27.6771.00 51.52 ATOM 5047 OE2 GLU B 837 43.394 24.512 25.552 1.00 51.73 ATOM5048 C GLU B 837 39.348 28.242 26.494 1.00 26.43 ATOM 5049 O GLU B 83738.902 28.413 27.628 1.00 27.28 ATOM 5050 N ASP B 838 39.819 29.23825.749 1.00 24.88 ATOM 5051 CA ASP B 838 39.846 30.604 26.254 1.00 25.77ATOM 5052 CB ASP B 838 40.811 31.457 25.428 1.00 38.63 ATOM 5053 CG ASPB 838 42.256 31.011 25.582 1.00 39.53 ATOM 5054 OD1 ASP B 838 42.76531.036 26.724 1.00 39.53 ATOM 5055 OD2 ASP B 838 42.877 30.633 24.5681.00 39.29 ATOM 5056 C ASP B 838 38.449 31.226 26.252 1.00 25.03 ATOM5057 O ASP B 838 38.277 32.360 26.699 1.00 25.25 ATOM 5058 N CYS B 83937.464 30.483 25.748 1.00 29.32 ATOM 5059 CA CYS B 839 36.073 30.94925.721 1.00 28.67 ATOM 5060 CB CYS B 839 35.383 30.561 24.400 1.00 25.46ATOM 5061 SG CYS B 839 35.809 31.580 22.967 1.00 23.35 ATOM 5062 C CYS B839 35.299 30.342 26.895 1.00 29.69 ATOM 5063 O CYS B 839 34.075 30.46826.984 1.00 29.52 ATOM 5064 N PHE B 840 36.023 29.686 27.798 1.00 26.11ATOM 5065 CA PHE B 840 35.405 29.055 28.960 1.00 25.54 ATOM 5066 CB PHEB 840 36.467 28.387 29.834 1.00 29.48 ATOM 5067 CG PHE B 840 35.91627.797 31.101 1.00 29.46 ATOM 5068 CD1 PHE B 840 35.084 26.679 31.0601.00 29.72 ATOM 5069 CD2 PHE B 840 36.204 28.373 32.333 1.00 29.95 ATOM5070 CE1 PHE B 840 34.546 26.143 32.231 1.00 30.22 ATOM 5071 CE2 PHE B840 35.671 27.845 33.512 1.00 29.42 ATOM 5072 CZ PHE B 840 34.840 26.72933.460 1.00 29.68 ATOM 5073 C PHE B 840 34.567 29.996 29.831 1.00 26.06ATOM 5074 O PHE B 840 33.531 29.593 30.354 1.00 26.34 ATOM 5075 N PRO B841 35.007 31.253 30.013 1.00 25.13 ATOM 5076 CD PRO B 841 36.255 31.90429.575 1.00 24.36 ATOM 5077 CA PRO B 841 34.210 32.164 30.846 1.00 24.99ATOM 5078 CB PRO B 841 34.927 33.502 30.673 1.00 24.78 ATOM 5079 CG PROB 841 36.368 33.073 30.535 1.00 24.46 ATOM 5080 C PRO B 841 32.72932.229 30.446 1.00 24.81 ATOM 5081 O PRO B 841 31.865 32.393 31.300 1.0025.33 ATOM 5082 N LEU B 842 32.435 32.096 29.155 1.00 24.08 ATOM 5083 CALEU B 842 31.044 32.143 28.707 1.00 22.49 ATOM 5084 CB LEU B 842 30.97232.171 27.177 1.00 19.33 ATOM 5085 CG LEU B 842 31.614 33.377 26.4881.00 20.20 ATOM 5086 CD1 LEU B 842 31.712 33.118 24.985 1.00 19.25 ATOM5087 CD2 LEU B 842 30.794 34.632 26.783 1.00 20.71 ATOM 5088 C LEU B 84230.260 30.944 29.242 1.00 22.87 ATOM 5089 O LEU B 842 29.143 31.08829.732 1.00 23.13 ATOM 5090 N LEU B 843 30.855 29.760 29.158 1.00 22.66ATOM 5091 CA LEU B 843 30.195 28.553 29.640 1.00 22.53 ATOM 5092 CB LEUB 843 31.032 27.317 29.298 1.00 33.57 ATOM 5093 CG LEU B 843 30.36625.935 29.275 1.00 34.94 ATOM 5094 CD1 LEU B 843 31.458 24.882 29.1571.00 34.20 ATOM 5095 CD2 LEU B 843 29.540 25.691 30.515 1.00 34.62 ATOM5096 C LEU B 843 30.024 28.635 31.153 1.00 22.75 ATOM 5097 O LEU B 84328.976 28.280 31.690 1.00 22.24 ATOM 5098 N ASP B 844 31.068 29.10131.831 1.00 25.80 ATOM 5099 CA ASP B 844 31.061 29.228 33.283 1.00 26.51ATOM 5100 CB ASP B 844 32.425 29.733 33.761 1.00 37.17 ATOM 5101 CG ASPB 844 32.584 29.653 35.267 1.00 37.71 ATOM 5102 OD1 ASP B 844 32.27728.589 35.844 1.00 37.75 ATOM 5103 OD2 ASP B 844 33.028 30.654 35.8711.00 38.29 ATOM 5104 C ASP B 844 29.953 30.171 33.750 1.00 26.88 ATOM5105 O ASP B 844 29.215 29.855 34.683 1.00 25.76 ATOM 5106 N GLY B 84529.840 31.323 33.093 1.00 27.19 ATOM 5107 CA GLY B 845 28.811 32.28133.457 1.00 27.20 ATOM 5108 C GLY B 845 27.418 31.719 33.239 1.00 27.51ATOM 5109 O GLY B 845 26.511 31.944 34.043 1.00 26.76 ATOM 5110 N CYS B846 27.246 30.982 32.147 1.00 23.86 ATOM 5111 CA CYS B 846 25.956 30.38131.838 1.00 24.52 ATOM 5112 CB CYS B 846 26.026 29.636 30.505 1.00 23.78ATOM 5113 SG CYS B 846 24.460 28.924 29.962 1.00 22.31 ATOM 5114 C CYS B846 25.538 29.414 32.938 1.00 24.60 ATOM 5115 O CYS B 846 24.388 29.41433.373 1.00 24.31 ATOM 5116 N ARG B 847 26.477 28.589 33.394 1.00 26.53ATOM 5117 CA ARG B 847 26.174 27.621 34.438 1.00 26.50 ATOM 5118 CB ARGB 847 27.317 26.605 34.556 1.00 46.23 ATOM 5119 CG ARG B 847 27.48625.797 33.273 1.00 46.99 ATOM 5120 CD ARG B 847 28.277 24.507 33.4431.00 47.45 ATOM 5121 NE ARG B 847 29.724 24.700 33.406 1.00 47.23 ATOM5122 CZ ARG B 847 30.594 23.737 33.111 1.00 47.33 ATOM 5123 NH1 ARG B847 30.165 22.517 32.822 1.00 47.47 ATOM 5124 NH2 ARG B 847 31.89623.989 33.109 1.00 46.97 ATOM 5125 C ARG B 847 25.893 28.301 35.776 1.0026.91 ATOM 5126 O ARG B 847 25.046 27.842 36.549 1.00 27.77 ATOM 5127 NLYS B 848 26.592 29.400 36.039 1.00 28.28 ATOM 5128 CA LYS B 848 26.38430.155 37.271 1.00 27.83 ATOM 5129 CB LYS B 848 27.420 31.277 37.3991.00 32.07 ATOM 5130 CG LYS B 848 28.831 30.798 37.731 1.00 32.23 ATOM5131 CD LYS B 848 29.798 31.975 37.858 1.00 32.55 ATOM 5132 CE LYS B 84831.198 31.513 38.248 1.00 32.52 ATOM 5133 NZ LYS B 848 32.179 32.64238.241 1.00 33.18 ATOM 5134 C LYS B 848 24.973 30.740 37.257 1.00 28.34ATOM 5135 O LYS B 848 24.291 30.758 38.282 1.00 28.54 ATOM 5136 N ASN B849 24.525 31.213 36.097 1.00 24.72 ATOM 5137 CA ASN B 849 23.179 31.76536.026 1.00 24.90 ATOM 5138 CB ASN B 849 22.975 32.558 34.734 1.00 24.86ATOM 5139 CG ASN B 849 23.561 33.949 34.817 1.00 25.77 ATOM 5140 OD1 ASNB 849 23.482 34.602 35.865 1.00 26.99 ATOM 5141 ND2 ASN B 849 24.13934.422 33.717 1.00 25.44 ATOM 5142 C ASN B 849 22.117 30.676 36.149 1.0024.90 ATOM 5143 O ASN B 849 21.041 30.909 36.698 1.00 25.65 ATOM 5144 NARG B 850 22.410 29.484 35.639 1.00 26.25 ATOM 5145 CA ARG B 850 21.45228.392 35.738 1.00 26.05 ATOM 5146 CB ARG B 850 21.991 27.128 35.0711.00 37.42 ATOM 5147 CG ARG B 850 21.057 25.945 35.237 1.00 37.84 ATOM5148 CD ARG B 850 21.721 24.635 34.879 1.00 37.92 ATOM 5149 NE ARG B 85020.875 23.509 35.261 1.00 38.86 ATOM 5150 CZ ARG B 850 19.666 23.28634.761 1.00 38.08 ATOM 5151 NH1 ARG B 850 19.168 24.114 33.854 1.0039.16 ATOM 5152 NH2 ARG B 850 18.950 22.247 35.172 1.00 37.88 ATOM 5153C ARG B 850 21.209 28.112 37.217 1.00 26.02 ATOM 5154 O ARG B 850 20.08727.861 37.646 1.00 25.93 ATOM 5155 N GLN B 851 22.290 28.148 37.986 1.0029.35 ATOM 5156 CA GLN B 851 22.231 27.915 39.419 1.00 29.80 ATOM 5157CB GLN B 851 23.641 28.042 40.006 1.00 57.33 ATOM 5158 CG GLN B 85123.706 28.453 41.467 1.00 58.18 ATOM 5159 CD GLN B 851 25.130 28.73141.920 1.00 58.63 ATOM 5160 OE1 GLN B 851 25.355 29.314 42.983 1.0058.50 ATOM 5161 NE2 GLN B 851 26.101 28.309 41.114 1.00 58.38 ATOM 5162C GLN B 851 21.289 28.920 40.068 1.00 29.02 ATOM 5163 O GLN B 851 20.41328.550 40.852 1.00 29.23 ATOM 5164 N LYS B 852 21.464 30.192 39.724 1.0028.14 ATOM 5165 CA LYS B 852 20.635 31.253 40.283 1.00 28.58 ATOM 5166CB LYS B 852 21.150 32.616 39.815 1.00 42.42 ATOM 5167 CG LYS B 85222.495 33.007 40.409 1.00 42.77 ATOM 5168 CD LYS B 852 22.371 33.23841.906 1.00 42.79 ATOM 5169 CE LYS B 852 23.700 33.633 42.527 1.00 43.26ATOM 5170 NZ LYS B 852 23.538 34.014 43.959 1.00 43.16 ATOM 5171 C LYS B852 19.153 31.116 39.941 1.00 28.34 ATOM 5172 O LYS B 852 18.296 31.25440.819 1.00 28.28 ATOM 5173 N TRP B 853 18.846 30.854 38.672 1.00 28.99ATOM 5174 CA TRP B 853 17.454 30.709 38.252 1.00 29.17 ATOM 5175 CB TRPB 853 17.355 30.629 36.719 1.00 25.14 ATOM 5176 CG TRP B 853 17.51731.963 36.032 1.00 23.87 ATOM 5177 CD2 TRP B 853 16.695 33.121 36.2101.00 23.86 ATOM 5178 CE2 TRP B 853 17.216 34.136 35.377 1.00 23.34 ATOM5179 CE3 TRP B 853 15.567 33.400 36.995 1.00 24.36 ATOM 5180 CD1 TRP B853 18.475 32.311 35.121 1.00 24.42 ATOM 5181 NE1 TRP B 853 18.30233.614 34.725 1.00 24.36 ATOM 5182 CZ2 TRP B 853 16.648 35.412 35.3051.00 23.69 ATOM 5183 CZ3 TRP B 853 15.002 34.669 36.924 1.00 23.64 ATOM5184 CH2 TRP B 853 15.545 35.657 36.085 1.00 24.37 ATOM 5185 C TRP B 85316.783 29.488 38.882 1.00 29.77 ATOM 5186 O TRP B 853 15.632 29.56139.309 1.00 29.78 ATOM 5187 N GLN B 854 17.504 28.371 38.946 1.00 29.55ATOM 5188 CA GLN B 854 16.951 27.150 39.526 1.00 30.02 ATOM 5189 CB GLNB 854 17.937 25.993 39.358 1.00 34.76 ATOM 5190 CG GLN B 854 17.45124.662 39.918 1.00 34.86 ATOM 5191 CD GLN B 854 16.141 24.207 39.3051.00 35.26 ATOM 5192 OE1 GLN B 854 15.984 24.197 38.085 1.00 35.00 ATOM5193 NE2 GLN B 854 15.195 23.815 40.151 1.00 35.46 ATOM 5194 C GLN B 85416.611 27.328 41.005 1.00 30.99 ATOM 5195 O GLN B 854 15.559 26.88441.462 1.00 30.12 ATOM 5196 N ALA B 855 17.501 27.976 41.748 1.00 37.27ATOM 5197 CA ALA B 855 17.270 28.206 43.171 1.00 38.24 ATOM 5198 CB ALAB 855 18.445 28.958 43.777 1.00 27.97 ATOM 5199 C ALA B 855 15.97628.988 43.380 1.00 38.50 ATOM 5200 O ALA B 855 15.308 28.840 44.404 1.0038.79 ATOM 5201 N LEU B 856 15.622 29.817 42.404 1.00 35.46 ATOM 5202 CALEU B 856 14.398 30.613 42.484 1.00 35.13 ATOM 5203 CB LEU B 856 14.50731.858 41.597 1.00 30.40 ATOM 5204 CG LEU B 856 15.541 32.924 41.9651.00 29.57 ATOM 5205 CD1 LEU B 856 15.493 34.056 40.956 1.00 30.17 ATOM5206 CD2 LEU B 856 15.266 33.443 43.367 1.00 30.22 ATOM 5207 C LEU B 85613.179 29.805 42.054 1.00 34.94 ATOM 5208 O LEU B 856 12.076 30.01242.555 1.00 34.78 ATOM 5209 N ALA B 857 13.385 28.876 41.127 1.00 36.42ATOM 5210 CA ALA B 857 12.299 28.055 40.609 1.00 36.87 ATOM 5211 CB ALAB 857 12.648 27.577 39.206 1.00 33.84 ATOM 5212 C ALA B 857 11.92626.859 41.482 1.00 37.18 ATOM 5213 O ALA B 857 10.774 26.429 41.482 1.0037.43 ATOM 5214 N GLU B 858 12.892 26.319 42.216 1.00 41.64 ATOM 5215 CAGLU B 858 12.634 25.161 43.069 1.00 42.85 ATOM 5216 CB GLU B 858 13.92124.368 43.295 1.00 56.15 ATOM 5217 CG GLU B 858 15.034 25.173 43.9301.00 56.44 ATOM 5218 CD GLU B 858 16.249 24.329 44.252 1.00 56.70 ATOM5219 OE1 GLU B 858 16.752 23.629 43.346 1.00 56.58 ATOM 5220 OE2 GLU B858 16.700 24.370 45.415 1.00 56.71 ATOM 5221 C GLU B 858 12.037 25.54144.416 1.00 42.83 ATOM 5222 O GLU B 858 11.799 26.744 44.645 1.00 42.70ATOM 5223 OXT GLU B 858 11.814 24.618 45.227 1.00 56.34 TER ATOM 5225 N1SIL A 1 −13.215 −5.663 26.629 1.00 24.07 ATOM 5226 C18 SIL A 1 −13.515−5.899 27.857 1.00 24.70 ATOM 5227 C19 SIL A 1 −14.726 −6.742 28.1461.00 24.74 ATOM 5228 C43 SIL A 1 −15.702 −6.365 29.114 1.00 25.67 ATOM5229 O44 SIL A 1 −15.506 −5.152 29.812 1.00 24.76 ATOM 5230 C45 SIL A 1−16.389 −4.626 30.824 1.00 25.28 ATOM 5231 C47 SIL A 1 −15.790 −3.29431.325 1.00 25.55 ATOM 5232 C41 SIL A 1 −16.830 −7.231 29.333 1.00 25.19ATOM 5233 C39 SIL A 1 −16.955 −8.443 28.594 1.00 26.15 ATOM 5234 C22 SILA 1 −15.963 −8.801 27.633 1.00 25.41 ATOM 5235 S23 SIL A 1 −16.074−10.311 26.687 1.00 26.04 ATOM 5236 O38 SIL A 1 −17.300 −10.973 27.1021.00 25.69 ATOM 5237 O37 SIL A 1 −14.845 −11.046 26.958 1.00 26.01 ATOM5238 N24 SIL A 1 −16.149 −10.048 25.039 1.00 26.05 ATOM 5239 C35 SIL A 1−17.168 −8.998 24.670 1.00 26.28 ATOM 5240 C33 SIL A 1 −17.218 −8.77223.126 1.00 26.30 ATOM 5241 N29 SIL A 1 −15.854 −8.482 22.563 1.00 26.54ATOM 5242 C31 SIL A 1 −15.924 −8.260 21.089 1.00 26.02 ATOM 5243 C27 SILA 1 −14.887 −9.587 22.889 1.00 26.44 ATOM 5244 C25 SIL A 1 −14.787−9.831 24.428 1.00 25.61 ATOM 5245 C20 SIL A 1 −14.868 −7.946 27.4271.00 25.44 ATOM 5246 N17 SIL A 1 −12.749 −5.402 28.877 1.00 24.74 ATOM5247 C15 SIL A 1 −11.635 −4.635 28.662 1.00 25.23 ATOM 5248 O16 SIL A 1−10.964 −4.202 29.580 1.00 24.95 ATOM 5249 C14 SIL A 1 −11.266 −4.35027.234 1.00 25.33 ATOM 5250 N11 SIL A 1 −10.297 −3.680 26.649 1.00 24.67ATOM 5251 C12 SIL A 1 −9.206 −2.961 27.299 1.00 25.39 ATOM 5252 N10 SILA 1 −10.467 −3.764 25.300 1.00 25.03 ATOM 5253 C3 SIL A 1 −11.495 −4.45525.004 1.00 24.25 ATOM 5254 C4 SIL A 1 −12.014 −4.783 23.619 1.00 25.73ATOM 5255 C6 SIL A 1 −12.905 −3.666 22.952 1.00 26.42 ATOM 5256 C8 SIL A1 −13.128 −2.379 23.800 1.00 25.69 ATOM 5257 C2 SIL A 1 −12.059 −4.86626.277 1.00 24.93 TER ATOM 5259 N1 SIL B 1 15.164 33.812 25.541 1.0025.10 ATOM 5260 C18 SIL B 1 14.895 33.565 26.769 1.00 24.27 ATOM 5261C19 SIL B 1 13.700 32.702 27.070 1.00 24.84 ATOM 5262 C43 SIL B 1 12.72933.045 28.058 1.00 24.56 ATOM 5263 O44 SIL B 1 12.899 34.250 28.780 1.0026.57 ATOM 5264 C45 SIL B 1 12.006 34.722 29.810 1.00 25.69 ATOM 5265C47 SIL B 1 12.558 36.064 30.336 1.00 25.09 ATOM 5266 C41 SIL B 1 11.62232.157 28.280 1.00 25.59 ATOM 5267 C39 SIL B 1 11.507 30.960 27.526 1.0025.77 ATOM 5268 C22 SIL B 1 12.487 30.633 26.544 1.00 25.79 ATOM 5269S23 SIL B 1 12.368 29.137 25.587 1.00 28.36 ATOM 5270 O38 SIL B 1 11.16428.457 26.018 1.00 26.14 ATOM 5271 O37 SIL B 1 13.594 28.402 25.827 1.0026.31 ATOM 5272 N24 SIL B 1 12.244 29.398 23.942 1.00 26.57 ATOM 5273C35 SIL B 1 11.267 30.495 23.609 1.00 25.93 ATOM 5274 C33 SIL B 1 11.16830.716 22.066 1.00 26.61 ATOM 5275 N29 SIL B 1 12.519 30.913 21.439 1.0026.95 ATOM 5276 C31 SIL B 1 12.402 31.132 19.969 1.00 25.72 ATOM 5277C27 SIL B 1 13.436 29.763 21.739 1.00 26.60 ATOM 5278 C25 SIL B 1 13.58329.525 23.276 1.00 26.54 ATOM 5279 C20 SIL B 1 13.569 31.507 26.332 1.0024.95 ATOM 5280 N17 SIL B 1 15.678 34.063 27.775 1.00 25.01 ATOM 5281C15 SIL B 1 16.778 34.843 27.541 1.00 25.62 ATOM 5282 O16 SIL B 1 17.47135.279 28.442 1.00 25.56 ATOM 5283 C14 SIL B 1 17.109 35.142 26.111 1.0024.85 ATOM 5284 N11 SIL B 1 18.054 35.828 25.516 1.00 24.72 ATOM 5285C12 SIL B 1 19.147 36.556 26.153 1.00 25.78 ATOM 5286 N10 SIL B 1 17.86335.755 24.172 1.00 25.21 ATOM 5287 C3 SIL B 1 16.841 35.056 23.885 1.0025.43 ATOM 5288 C4 SIL B 1 16.304 34.734 22.500 1.00 25.15 ATOM 5289 C6SIL B 1 15.454 35.880 21.819 1.00 26.50 ATOM 5290 C8 SIL B 1 15.28437.187 22.646 1.00 26.25 ATOM 5291 C2 SIL B 1 16.305 34.627 25.167 1.0024.69 TER ATOM 5293 ZN ZN A 864 −8.302 0.061 19.726 1.00 33.93 ATOM 5294MG MG A 865 −10.882 −0.915 17.074 1.00 20.57 TER ATOM 5296 ZN ZN B 86419.969 39.499 18.508 1.00 25.29 ATOM 5297 MG MG B 865 0.014 0.254 −1.2831.00 32.82 END

[0216] TABLE 4 Atomic coordinates for PDE5* apo protein Atom Number,Atom Type, Residue Type, Residue Number Cartesian Coordinates X, Y, Z,Atom Occupancy (O), Temperature Factor (B) X Y Z O B ATOM 1 CB GLU A 5369.887 25.182 24.787 1.00 33.98 ATOM 2 CG GLU A 536 11.305 25.697 24.6351.00 42.32 ATOM 3 CD GLU A 536 11.492 27.074 25.245 1.00 47.12 ATOM 4OE1 GLU A 536 11.290 27.223 26.470 1.00 54.45 ATOM 5 OE2 GLU A 53611.842 28.012 24.499 1.00 51.15 ATOM 6 C GLU A 536 7.942 25.044 26.3271.00 37.22 ATOM 7 O GLU A 536 7.222 24.272 25.690 1.00 36.76 ATOM 8 NGLU A 536 9.991 23.667 26.752 1.00 36.93 ATOM 9 CA GLU A 536 9.45624.961 26.239 1.00 37.47 ATOM 10 N THR A 537 7.463 25.990 27.125 1.0037.34 ATOM 11 CA THR A 537 6.035 26.189 27.289 1.00 36.78 ATOM 12 CB THRA 537 5.750 27.235 28.387 1.00 43.61 ATOM 13 OG1 THR A 537 6.425 28.45728.069 1.00 45.23 ATOM 14 CG2 THR A 537 6.241 26.731 29.739 1.00 34.90ATOM 15 C THR A 537 5.452 26.660 25.957 1.00 35.15 ATOM 16 O THR A 5374.239 26.661 25.764 1.00 34.30 ATOM 17 N ARG A 538 6.336 27.046 25.0401.00 32.72 ATOM 18 CA ARG A 538 5.943 27.514 23.712 1.00 31.35 ATOM 19CB ARG A 538 7.143 28.133 23.002 1.00 33.78 ATOM 20 CG ARG A 538 6.91028.452 21.531 1.00 42.77 ATOM 21 CD ARG A 538 6.041 29.690 21.340 1.0051.85 ATOM 22 NE ARG A 538 4.638 29.475 21.687 1.00 50.21 ATOM 23 CZ ARGA 538 3.715 30.433 21.672 1.00 49.57 ATOM 24 NH1 ARG A 538 4.047 31.67321.330 1.00 48.08 ATOM 25 NH2 ARG A 538 2.458 30.154 21.992 1.00 49.14ATOM 26 C ARG A 538 5.405 26.369 22.861 1.00 30.33 ATOM 27 O ARG A 5384.381 26.501 22.187 1.00 28.72 ATOM 28 N GLU A 539 6.120 25.250 22.8761.00 28.94 ATOM 29 CA GLU A 539 5.709 24.080 22.115 1.00 25.47 ATOM 30CB GLU A 539 6.807 23.024 22.141 1.00 30.35 ATOM 31 CG GLU A 539 8.05523.426 21.391 1.00 31.75 ATOM 32 CD GLU A 539 9.188 22.463 21.628 1.0031.48 ATOM 33 OE1 GLU A 539 9.689 22.410 22.771 1.00 46.55 ATOM 34 OE2GLU A 539 9.575 21.754 20.676 1.00 57.06 ATOM 35 C GLU A 539 4.43723.511 22.718 1.00 23.49 ATOM 36 O GLU A 539 3.599 22.952 22.011 1.0021.01 ATOM 37 N LEU A 540 4.299 23.653 24.032 1.00 22.37 ATOM 38 CA LEUA 540 3.114 23.159 24.713 1.00 22.10 ATOM 39 CB LEU A 540 3.302 23.22326.231 1.00 19.44 ATOM 40 CG LEU A 540 2.098 22.763 27.059 1.00 22.04ATOM 41 CD1 LEU A 540 1.686 21.365 26.627 1.00 19.81 ATOM 42 CD2 LEU A540 2.441 22.783 28.539 1.00 38.12 ATOM 43 C LEU A 540 1.907 23.99524.300 1.00 21.23 ATOM 44 O LEU A 540 0.844 23.461 23.990 1.00 19.37ATOM 45 N GLN A 541 2.074 25.313 24.283 1.00 20.36 ATOM 46 CA GLN A 5410.972 26.185 23.905 1.00 18.42 ATOM 47 CB GLN A 541 1.410 27.651 23.9661.00 20.67 ATOM 48 CG GLN A 541 1.873 28.081 25.350 1.00 24.12 ATOM 49CD GLN A 541 2.356 29.519 25.401 1.00 24.37 ATOM 50 OE1 GLN A 541 3.04729.986 24.497 1.00 17.86 ATOM 51 NE2 GLN A 541 2.008 30.223 26.474 1.0020.12 ATOM 52 C GLN A 541 0.477 25.833 22.505 1.00 17.74 ATOM 53 O GLN A541 −0.726 25.799 22.254 1.00 19.08 ATOM 54 N SER A 542 1.404 25.55221.596 1.00 15.82 ATOM 55 CA SER A 542 1.026 25.207 20.231 1.00 18.42ATOM 56 CB SER A 542 2.263 25.179 19.329 1.00 20.91 ATOM 57 OG SER A 5422.857 26.463 19.251 1.00 37.22 ATOM 58 C SER A 542 0.320 23.858 20.1741.00 16.82 ATOM 59 O SER A 542 −0.710 23.709 19.520 1.00 17.71 ATOM 60 NLEU A 543 0.875 22.874 20.872 1.00 17.64 ATOM 61 CA LEU A 543 0.29721.538 20.878 1.00 17.88 ATOM 62 CB LEU A 543 1.269 20.550 21.531 1.0013.54 ATOM 63 CG LEU A 543 0.762 19.113 21.695 1.00 17.02 ATOM 64 CD1LEU A 543 0.501 18.504 20.329 1.00 14.15 ATOM 65 CD2 LEU A 543 1.78918.284 22.465 1.00 10.59 ATOM 66 C LEU A 543 −1.049 21.468 21.592 1.0018.33 ATOM 67 O LEU A 543 −2.013 20.914 21.064 1.00 19.18 ATOM 68 N ALAA 544 −1.112 22.038 22.790 1.00 18.60 ATOM 69 CA ALA A 544 −2.332 22.00323.588 1.00 19.09 ATOM 70 CB ALA A 544 −2.053 22.573 24.972 1.00 17.83ATOM 71 C ALA A 544 −3.527 22.717 22.967 1.00 21.56 ATOM 72 O ALA A 544−4.667 22.306 23.165 1.00 23.51 ATOM 73 N ALA A 545 −3.269 23.782 22.2171.00 23.98 ATOM 74 CA ALA A 545 −4.348 24.547 21.599 1.00 24.34 ATOM 75CB ALA A 545 −3.861 25.952 21.274 1.00 26.53 ATOM 76 C ALA A 545 −4.90123.891 20.341 1.00 25.76 ATOM 77 O ALA A 545 −6.065 24.079 19.992 1.0028.16 ATOM 78 N ALA A 546 −4.059 23.115 19.668 1.00 24.74 ATOM 79 CA ALAA 546 −4.441 22.443 18.430 1.00 24.22 ATOM 80 CB ALA A 546 −3.239 21.70117.861 1.00 22.00 ATOM 81 C ALA A 546 −5.621 21.485 18.529 1.00 21.89ATOM 82 O ALA A 546 −5.803 20.791 19.529 1.00 23.27 ATOM 83 N VAL A 547−6.433 21.464 17.478 1.00 21.72 ATOM 84 CA VAL A 547 −7.560 20.54817.418 1.00 21.65 ATOM 85 CB VAL A 547 −8.660 21.045 16.454 1.00 23.33ATOM 86 CG1 VAL A 547 −9.754 19.993 16.326 1.00 25.11 ATOM 87 CG2 VAL A547 −9.250 22.355 16.965 1.00 23.58 ATOM 88 C VAL A 547 −6.925 19.28416.850 1.00 22.28 ATOM 89 O VAL A 547 −6.280 19.329 15.805 1.00 24.96ATOM 90 N VAL A 548 −7.090 18.165 17.542 1.00 21.82 ATOM 91 CA VAL A 548−6.498 16.909 17.098 1.00 19.25 ATOM 92 CB VAL A 548 −6.387 15.92518.278 1.00 19.56 ATOM 93 CG1 VAL A 548 −5.669 14.659 17.840 1.00 23.78ATOM 94 CG2 VAL A 548 −5.656 16.593 19.438 1.00 24.95 ATOM 95 C VAL A548 −7.284 16.241 15.975 1.00 17.26 ATOM 96 O VAL A 548 −8.453 15.90416.146 1.00 19.24 ATOM 97 N PRO A 549 −6.646 16.038 14.808 1.00 17.33ATOM 98 CD PRO A 549 −5.293 16.478 14.431 1.00 18.64 ATOM 99 CA PRO A549 −7.315 15.401 13.670 1.00 19.43 ATOM 100 CB PRO A 549 −6.245 15.42512.575 1.00 17.30 ATOM 101 CG PRO A 549 −5.420 16.615 12.931 1.00 23.24ATOM 102 C PRO A 549 −7.742 13.982 14.023 1.00 20.23 ATOM 103 O PRO A549 −7.259 13.402 15.001 1.00 16.82 ATOM 104 N SER A 550 −8.645 13.43113.220 1.00 17.57 ATOM 105 CA SER A 550 −9.153 12.081 13.432 1.00 20.68ATOM 106 CB SER A 550 −10.343 11.822 12.512 1.00 17.19 ATOM 107 OG SER A550 −9.934 11.861 11.153 1.00 18.60 ATOM 108 C SER A 550 −8.075 11.05513.127 1.00 17.34 ATOM 109 O SER A 550 −7.096 11.357 12.443 1.00 16.71ATOM 110 N ALA A 551 −8.257 9.841 13.637 1.00 18.46 ATOM 111 CA ALA A551 −7.304 8.769 13.380 1.00 19.34 ATOM 112 CB ALA A 551 −7.706 7.50714.143 1.00 17.06 ATOM 113 C ALA A 551 −7.322 8.502 11.879 1.00 18.62ATOM 114 O ALA A 551 −6.284 8.262 11.261 1.00 20.73 ATOM 115 N GLN A 552−8.518 8.554 11.300 1.00 19.78 ATOM 116 CA GLN A 552 −8.700 8.327 9.8691.00 21.36 ATOM 117 CB GLN A 552 −10.175 8.528 9.502 1.00 23.40 ATOM 118CG GLN A 552 −10.541 8.181 8.067 1.00 31.79 ATOM 119 CD GLN A 552−12.026 8.358 7.797 1.00 35.80 ATOM 120 OE1 GLN A 552 −12.864 7.6758.390 1.00 46.36 ATOM 121 NE2 GLN A 552 −12.358 9.283 6.902 1.00 49.03ATOM 122 C GLN A 552 −7.820 9.301 9.086 1.00 21.35 ATOM 123 O GLN A 552−7.040 8.897 8.219 1.00 21.48 ATOM 124 N THR A 553 −7.938 10.584 9.4081.00 19.75 ATOM 125 CA THR A 553 −7.151 11.612 8.739 1.00 19.52 ATOM 126CB THR A 553 −7.501 13.017 9.268 1.00 18.18 ATOM 127 OG1 THR A 553−8.871 13.318 8.971 1.00 19.96 ATOM 128 CG2 THR A 553 −6.597 14.0668.627 1.00 18.92 ATOM 129 C THR A 553 −5.654 11.396 8.926 1.00 20.00ATOM 130 O THR A 553 −4.875 11.523 7.980 1.00 19.53 ATOM 131 N LEU A 554−5.260 11.062 10.150 1.00 19.10 ATOM 132 CA LEU A 554 −3.855 10.85310.474 1.00 20.03 ATOM 133 CB LEU A 554 −3.650 10.974 11.987 1.00 17.91ATOM 134 CG LEU A 554 −4.091 12.323 12.571 1.00 18.40 ATOM 135 CD1 LEU A554 −3.972 12.316 14.082 1.00 16.11 ATOM 136 CD2 LEU A 554 −3.237 13.43611.977 1.00 23.68 ATOM 137 C LEU A 554 −3.303 9.521 9.970 1.00 19.88ATOM 138 O LEU A 554 −2.093 9.304 9.994 1.00 19.74 ATOM 139 N LYS A 555−4.198 8.637 9.533 1.00 17.37 ATOM 140 CA LYS A 555 −3.833 7.327 8.9971.00 19.69 ATOM 141 CB LYS A 555 −3.032 7.523 7.708 1.00 26.45 ATOM 142CG LYS A 555 −3.740 8.429 6.708 1.00 33.54 ATOM 143 CD LYS A 555 −2.8298.837 5.565 1.00 36.95 ATOM 144 CE LYS A 555 −3.542 9.803 4.633 1.0036.53 ATOM 145 NZ LYS A 555 −2.645 10.308 3.562 1.00 43.43 ATOM 146 CLYS A 555 −3.043 6.454 9.976 1.00 19.45 ATOM 147 O LYS A 555 −2.2945.569 9.565 1.00 18.29 ATOM 148 N ILE A 556 −3.227 6.688 11.271 1.0017.06 ATOM 149 CA ILE A 556 −2.501 5.917 12.273 1.00 16.83 ATOM 150 CBILE A 556 −2.475 6.638 13.641 1.00 13.95 ATOM 151 CG2 ILE A 556 −1.5657.856 13.569 1.00 16.87 ATOM 152 CG1 ILE A 556 −3.897 7.017 14.062 1.0014.93 ATOM 153 CD1 ILE A 556 −3.981 7.598 15.460 1.00 19.73 ATOM 154 CILE A 556 −3.019 4.496 12.489 1.00 14.60 ATOM 155 O ILE A 556 −2.4433.745 13.271 1.00 12.74 ATOM 156 N THR A 557 −4.099 4.125 11.806 1.0014.27 ATOM 157 CA THR A 557 −4.653 2.776 11.938 1.00 15.05 ATOM 158 CBTHR A 557 −6.187 2.772 11.699 1.00 21.22 ATOM 159 OG1 THR A 557 −6.8133.726 12.567 1.00 20.77 ATOM 160 CG2 THR A 557 −6.773 1.398 11.982 1.0021.26 ATOM 161 C THR A 557 −3.991 1.855 10.907 1.00 14.39 ATOM 162 O THRA 557 −4.131 0.631 10.955 1.00 16.89 ATOM 163 N ASP A 558 −3.257 2.4569.979 1.00 14.56 ATOM 164 CA ASP A 558 −2.593 1.702 8.923 1.00 14.77ATOM 165 CB ASP A 558 −2.374 2.613 7.713 1.00 20.77 ATOM 166 CG ASP A558 −3.648 3.312 7.274 1.00 30.09 ATOM 167 OD1 ASP A 558 −4.657 2.6167.031 1.00 38.75 ATOM 168 OD2 ASP A 558 −3.642 4.555 7.173 1.00 46.69ATOM 169 C ASP A 558 −1.258 1.086 9.351 1.00 14.68 ATOM 170 O ASP A 558−0.365 1.787 9.829 1.00 13.87 ATOM 171 N PHE A 559 −1.124 −0.227 9.1751.00 13.82 ATOM 172 CA PHE A 559 0.119 −0.916 9.526 1.00 13.07 ATOM 173CB PHE A 559 0.000 −2.427 9.283 1.00 14.41 ATOM 174 CG PHE A 559 −0.732−3.175 10.366 1.00 18.21 ATOM 175 CD1 PHE A 559 −0.289 −3.134 11.6801.00 14.30 ATOM 176 CD2 PHE A 559 −1.836 −3.960 10.060 1.00 16.61 ATOM177 CE1 PHE A 559 −0.931 −3.866 12.668 1.00 15.41 ATOM 178 CE2 PHE A 559−2.482 −4.692 11.043 1.00 15.41 ATOM 179 CZ PHE A 559 −2.031 −4.64712.344 1.00 12.10 ATOM 180 C PHE A 559 1.277 −0.386 8.680 1.00 11.71ATOM 181 O PHE A 559 2.431 −0.411 9.109 1.00 12.25 ATOM 182 N SER A 5600.965 0.079 7.473 1.00 13.82 ATOM 183 CA SER A 560 1.979 0.597 6.5551.00 13.86 ATOM 184 CB SER A 560 1.538 0.384 5.106 1.00 19.52 ATOM 185OG SER A 560 1.411 −0.996 4.816 1.00 19.35 ATOM 186 C SER A 560 2.2942.071 6.770 1.00 12.88 ATOM 187 O SER A 560 2.959 2.698 5.945 1.00 14.29ATOM 188 N PHE A 561 1.815 2.608 7.886 1.00 12.82 ATOM 189 CA PHE A 5612.021 4.009 8.261 1.00 13.63 ATOM 190 CB PHE A 561 1.567 4.207 9.7131.00 14.59 ATOM 191 CG PHE A 561 1.835 5.583 10.258 1.00 12.08 ATOM 192CD1 PHE A 561 0.956 6.625 10.014 1.00 17.74 ATOM 193 CD2 PHE A 561 2.9675.829 11.022 1.00 10.31 ATOM 194 CE1 PHE A 561 1.199 7.891 10.524 1.0021.75 ATOM 195 CE2 PHE A 561 3.220 7.093 11.537 1.00 13.27 ATOM 196 CZPHE A 561 2.333 8.126 11.287 1.00 18.85 ATOM 197 C PHE A 561 3.466 4.4988.125 1.00 14.38 ATOM 198 O PHE A 561 4.413 3.791 8.485 1.00 11.10 ATOM199 N SER A 562 3.625 5.716 7.607 1.00 14.38 ATOM 200 CA SER A 562 4.9396.334 7.453 1.00 13.72 ATOM 201 CB SER A 562 5.283 6.520 5.972 1.0015.96 ATOM 202 OG SER A 562 6.542 7.159 5.835 1.00 23.25 ATOM 203 C SERA 562 4.940 7.695 8.159 1.00 12.53 ATOM 204 O SER A 562 4.009 8.4908.014 1.00 12.55 ATOM 205 N ASP A 563 5.992 7.965 8.922 1.00 13.45 ATOM206 CA ASP A 563 6.094 9.223 9.661 1.00 15.79 ATOM 207 CB ASP A 5636.662 8.953 11.050 1.00 13.73 ATOM 208 CG ASP A 563 8.166 8.765 11.0221.00 15.49 ATOM 209 OD1 ASP A 563 8.895 9.680 11.465 1.00 18.81 ATOM 210OD2 ASP A 563 8.625 7.712 10.537 1.00 16.12 ATOM 211 C ASP A 563 7.00910.232 8.974 1.00 16.63 ATOM 212 O ASP A 563 7.112 11.383 9.404 1.0017.82 ATOM 213 N PHE A 564 7.673 9.796 7.911 1.00 16.51 ATOM 214 CA PHEA 564 8.633 10.635 7.205 1.00 18.23 ATOM 215 CB PHE A 564 9.207 9.8716.011 1.00 15.87 ATOM 216 CG PHE A 564 10.446 10.494 5.438 1.00 26.61ATOM 217 CD1 PHE A 564 11.599 10.592 6.201 1.00 20.64 ATOM 218 CD2 PHE A564 10.458 10.991 4.144 1.00 27.32 ATOM 219 CE1 PHE A 564 12.742 11.1745.685 1.00 30.38 ATOM 220 CE2 PHE A 564 11.599 11.574 3.622 1.00 33.45ATOM 221 CZ PHE A 564 12.742 11.665 4.394 1.00 33.80 ATOM 222 C PHE A564 8.157 12.010 6.740 1.00 18.52 ATOM 223 O PHE A 564 8.942 12.9596.728 1.00 19.54 ATOM 224 N GLU A 565 6.885 12.122 6.369 1.00 16.14 ATOM225 CA GLU A 565 6.340 13.391 5.890 1.00 19.03 ATOM 226 CB GLU A 5655.277 13.142 4.813 1.00 18.54 ATOM 227 CG GLU A 565 5.708 12.238 3.6681.00 33.46 ATOM 228 CD GLU A 565 6.004 10.818 4.117 1.00 40.92 ATOM 229OE1 GLU A 565 5.205 10.258 4.899 1.00 41.02 ATOM 230 OE2 GLU A 565 7.03210.259 3.680 1.00 50.71 ATOM 231 C GLU A 565 5.710 14.229 7.002 1.0019.43 ATOM 232 O GLU A 565 5.158 15.301 6.740 1.00 20.33 ATOM 233 N LEUA 566 5.786 13.746 8.238 1.00 13.91 ATOM 234 CA LEU A 566 5.193 14.4639.362 1.00 15.26 ATOM 235 CB LEU A 566 4.515 13.482 10.321 1.00 15.63ATOM 236 CG LEU A 566 3.329 12.669 9.799 1.00 24.63 ATOM 237 CD1 LEU A566 2.864 11.698 10.881 1.00 23.72 ATOM 238 CD2 LEU A 566 2.199 13.6079.399 1.00 33.15 ATOM 239 C LEU A 566 6.187 15.306 10.147 1.00 14.43ATOM 240 O LEU A 566 7.358 14.960 10.265 1.00 17.81 ATOM 241 N SER A 5675.699 16.419 10.685 1.00 14.78 ATOM 242 CA SER A 567 6.517 17.317 11.4861.00 14.98 ATOM 243 CB SER A 567 5.928 18.727 11.467 1.00 21.89 ATOM 244OG SER A 567 4.679 18.752 12.144 1.00 17.63 ATOM 245 C SER A 567 6.49216.797 12.922 1.00 13.89 ATOM 246 O SER A 567 5.654 15.963 13.268 1.0013.82 ATOM 247 N ASP A 568 7.403 17.289 13.753 1.00 15.43 ATOM 248 CAASP A 568 7.428 16.869 15.149 1.00 15.57 ATOM 249 CB ASP A 568 8.53617.603 15.904 1.00 19.60 ATOM 250 CG ASP A 568 9.888 16.947 15.727 1.0016.75 ATOM 251 OD1 ASP A 568 9.989 16.021 14.899 1.00 19.05 ATOM 252 OD2ASP A 568 10.848 17.355 16.415 1.00 23.47 ATOM 253 C ASP A 568 6.07617.145 15.805 1.00 16.52 ATOM 254 O ASP A 568 5.559 16.313 16.556 1.0015.97 ATOM 255 N LEU A 569 5.505 18.311 15.516 1.00 15.09 ATOM 256 CALEU A 569 4.213 18.683 16.076 1.00 15.08 ATOM 257 CB LEU A 569 3.81520.093 15.620 1.00 16.05 ATOM 258 CG LEU A 569 2.385 20.516 15.974 1.0023.47 ATOM 259 CD1 LEU A 569 2.203 20.527 17.489 1.00 21.65 ATOM 260 CD2LEU A 569 2.103 21.896 15.398 1.00 27.54 ATOM 261 C LEU A 569 3.13617.694 15.647 1.00 12.90 ATOM 262 O LEU A 569 2.279 17.308 16.441 1.0016.26 ATOM 263 N GLU A 570 3.184 17.281 14.386 1.00 13.40 ATOM 264 CAGLU A 570 2.202 16.340 13.869 1.00 14.08 ATOM 265 CB GLU A 570 2.35416.196 12.352 1.00 14.43 ATOM 266 CG GLU A 570 1.885 17.432 11.579 1.0020.85 ATOM 267 CD GLU A 570 2.062 17.291 10.081 1.00 23.63 ATOM 268 OE1GLU A 570 3.218 17.158 9.632 1.00 21.68 ATOM 269 OE2 GLU A 570 1.04717.311 9.352 1.00 28.09 ATOM 270 C GLU A 570 2.309 14.978 14.547 1.0014.43 ATOM 271 O GLU A 570 1.293 14.319 14.780 1.00 15.20 ATOM 272 N THRA 571 3.529 14.551 14.866 1.00 12.67 ATOM 273 CA THR A 571 3.694 13.25915.538 1.00 12.83 ATOM 274 CB THR A 571 5.182 12.816 15.638 1.00 13.30ATOM 275 OG1 THR A 571 5.915 13.737 16.452 1.00 12.68 ATOM 276 CG2 THR A571 5.817 12.738 14.250 1.00 12.38 ATOM 277 C THR A 571 3.110 13.36016.945 1.00 11.29 ATOM 278 O THR A 571 2.589 12.381 17.483 1.00 12.14ATOM 279 N ALA A 572 3.202 14.548 17.538 1.00 12.42 ATOM 280 CA ALA A572 2.659 14.780 18.869 1.00 11.84 ATOM 281 CB ALA A 572 3.090 16.14219.388 1.00 12.18 ATOM 282 C ALA A 572 1.136 14.701 18.803 1.00 13.34ATOM 283 O ALA A 572 0.500 14.128 19.683 1.00 11.72 ATOM 284 N LEU A 5730.554 15.283 17.758 1.00 12.67 ATOM 285 CA LEU A 573 −0.894 15.24417.583 1.00 13.98 ATOM 286 CB LEU A 573 −1.307 16.104 16.384 1.00 14.33ATOM 287 CG LEU A 573 −1.135 17.619 16.544 1.00 14.55 ATOM 288 CD1 LEU A573 −1.445 18.310 15.224 1.00 21.57 ATOM 289 CD2 LEU A 573 −2.061 18.12517.647 1.00 20.27 ATOM 290 C LEU A 573 −1.338 13.795 17.366 1.00 15.26ATOM 291 O LEU A 573 −2.394 13.378 17.853 1.00 15.01 ATOM 292 N CYS A574 −0.534 13.030 16.632 1.00 13.44 ATOM 293 CA CYS A 574 −0.852 11.62516.385 1.00 13.06 ATOM 294 CB CYS A 574 0.187 10.974 15.470 1.00 12.27ATOM 295 SG CYS A 574 0.049 11.382 13.714 1.00 15.24 ATOM 296 C CYS A574 −0.873 10.864 17.703 1.00 12.15 ATOM 297 O CYS A 574 −1.710 9.99117.919 1.00 13.51 ATOM 298 N THR A 575 0.066 11.194 18.581 1.00 11.60ATOM 299 CA THR A 575 0.158 10.532 19.872 1.00 12.28 ATOM 300 CB THR A575 1.453 10.949 20.592 1.00 10.90 ATOM 301 OG1 THR A 575 2.575 10.57619.777 1.00 13.47 ATOM 302 CG2 THR A 575 1.565 10.264 21.944 1.00 10.06ATOM 303 C THR A 575 −1.068 10.841 20.726 1.00 11.74 ATOM 304 O THR A575 −1.613 9.952 21.379 1.00 10.78 ATOM 305 N ILE A 576 −1.514 12.09520.717 1.00 12.29 ATOM 306 CA ILE A 576 −2.700 12.453 21.484 1.00 11.92ATOM 307 CB ILE A 576 −3.046 13.945 21.354 1.00 11.38 ATOM 308 CG2 ILE A576 −4.371 14.222 22.053 1.00 12.83 ATOM 309 CG1 ILE A 576 −1.933 14.80221.965 1.00 17.73 ATOM 310 CD1 ILE A 576 −2.154 16.292 21.798 1.00 13.34ATOM 311 C ILE A 576 −3.880 11.636 20.960 1.00 12.34 ATOM 312 O ILE A576 −4.674 11.103 21.737 1.00 13.64 ATOM 313 N ARG A 577 −3.985 11.53219.638 1.00 13.14 ATOM 314 CA ARG A 577 −5.071 10.772 19.032 1.00 13.22ATOM 315 CB ARG A 577 −5.029 10.888 17.503 1.00 12.21 ATOM 316 CG ARG A577 −6.113 10.084 16.795 1.00 12.42 ATOM 317 CD ARG A 577 −7.492 10.38317.365 1.00 10.79 ATOM 318 NE ARG A 577 −7.912 11.757 17.111 1.00 18.46ATOM 319 CZ ARG A 577 −9.015 12.304 17.612 1.00 16.47 ATOM 320 NH1 ARG A577 −9.319 13.564 17.325 1.00 24.31 ATOM 321 NH2 ARG A 577 −9.809 11.59618.405 1.00 18.21 ATOM 322 C ARG A 577 −5.029 9.304 19.455 1.00 12.45ATOM 323 O ARG A 577 −6.069 8.675 19.625 1.00 11.98 ATOM 324 N MET A 578−3.831 8.756 19.630 1.00 10.43 ATOM 325 CA MET A 578 −3.716 7.367 20.0581.00 11.28 ATOM 326 CB MET A 578 −2.245 6.934 20.090 1.00 11.91 ATOM 327CG MET A 578 −1.605 6.808 18.716 1.00 12.93 ATOM 328 SD MET A 578 0.1346.324 18.830 1.00 16.07 ATOM 329 CE MET A 578 0.781 7.021 17.300 1.0019.76 ATOM 330 C MET A 578 −4.332 7.191 21.445 1.00 12.18 ATOM 331 O META 578 −5.103 6.260 21.675 1.00 11.26 ATOM 332 N PHE A 579 −3.982 8.08022.372 1.00 11.60 ATOM 333 CA PHE A 579 −4.521 8.004 23.725 1.00 11.60ATOM 334 CB PHE A 579 −3.921 9.097 24.619 1.00 12.17 ATOM 335 CG PHE A579 −2.584 8.748 25.201 1.00 9.68 ATOM 336 CD1 PHE A 579 −1.415 9.02324.510 1.00 13.42 ATOM 337 CD2 PHE A 579 −2.497 8.148 26.450 1.00 12.49ATOM 338 CE1 PHE A 579 −0.178 8.709 25.054 1.00 10.87 ATOM 339 CE2 PHE A579 −1.264 7.829 27.000 1.00 13.01 ATOM 340 CZ PHE A 579 −0.103 8.11326.301 1.00 12.83 ATOM 341 C PHE A 579 −6.040 8.170 23.708 1.00 12.84ATOM 342 O PHE A 579 −6.765 7.429 24.367 1.00 12.73 ATOM 343 N THR A 580−6.504 9.151 22.943 1.00 15.04 ATOM 344 CA THR A 580 −7.926 9.459 22.8391.00 14.30 ATOM 345 CB THR A 580 −8.145 10.702 21.967 1.00 10.78 ATOM346 OG1 THR A 580 −7.344 11.780 22.469 1.00 18.08 ATOM 347 CG2 THR A 580−9.610 11.115 21.987 1.00 13.16 ATOM 348 C THR A 580 −8.772 8.327 22.2731.00 14.34 ATOM 349 O THR A 580 −9.774 7.936 22.871 1.00 14.67 ATOM 350N ASP A 581 −8.367 7.806 21.119 1.00 15.75 ATOM 351 CA ASP A 581 −9.1066.731 20.466 1.00 14.61 ATOM 352 CB ASP A 581 −8.724 6.668 18.990 1.0016.27 ATOM 353 CG ASP A 581 −9.398 7.757 18.181 1.00 20.38 ATOM 354 OD1ASP A 581 −9.762 8.797 18.776 1.00 15.70 ATOM 355 OD2 ASP A 581 −9.5607.580 16.958 1.00 17.57 ATOM 356 C ASP A 581 −8.970 5.365 21.123 1.0015.19 ATOM 357 O ASP A 581 −9.627 4.402 20.719 1.00 14.62 ATOM 358 N LEUA 582 −8.110 5.275 22.130 1.00 13.55 ATOM 359 CA LEU A 582 −7.957 4.03222.867 1.00 14.36 ATOM 360 CB LEU A 582 −6.484 3.739 23.156 1.00 16.24ATOM 361 CG LEU A 582 −5.770 3.024 22.006 1.00 14.56 ATOM 362 CD1 LEU A582 −4.272 2.968 22.250 1.00 12.82 ATOM 363 CD2 LEU A 582 −6.351 1.62521.865 1.00 12.05 ATOM 364 C LEU A 582 −8.739 4.189 24.168 1.00 17.31ATOM 365 O LEU A 582 −8.617 3.378 25.081 1.00 17.82 ATOM 366 N ASN A 583−9.533 5.255 24.246 1.00 17.93 ATOM 367 CA ASN A 583 −10.361 5.50025.420 1.00 21.01 ATOM 368 CB ASN A 583 −11.405 4.377 25.525 1.00 22.07ATOM 369 CG ASN A 583 −12.368 4.564 26.682 1.00 34.95 ATOM 370 OD1 ASN A583 −12.921 5.645 26.879 1.00 34.93 ATOM 371 ND2 ASN A 583 −12.589 3.49627.444 1.00 39.94 ATOM 372 C ASN A 583 −9.516 5.575 26.693 1.00 23.16ATOM 373 O ASN A 583 −9.866 4.978 27.713 1.00 27.41 ATOM 374 N LEU A 584−8.406 6.313 26.634 1.00 18.24 ATOM 375 CA LEU A 584 −7.517 6.446 27.7911.00 18.39 ATOM 376 CB LEU A 584 −6.060 6.188 27.379 1.00 13.74 ATOM 377CG LEU A 584 −5.713 4.823 26.778 1.00 13.61 ATOM 378 CD1 LEU A 584−4.226 4.789 26.412 1.00 16.18 ATOM 379 CD2 LEU A 584 −6.050 3.72627.769 1.00 15.78 ATOM 380 C LEU A 584 −7.591 7.807 28.486 1.00 18.85ATOM 381 O LEU A 584 −7.377 7.904 29.695 1.00 18.54 ATOM 382 N VAL A 585−7.890 8.853 27.721 1.00 18.53 ATOM 383 CA VAL A 585 −7.956 10.21128.258 1.00 20.90 ATOM 384 CB VAL A 585 −8.157 11.234 27.123 1.00 25.63ATOM 385 CG1 VAL A 585 −8.083 12.648 27.672 1.00 26.57 ATOM 386 CG2 VALA 585 −7.102 11.024 26.054 1.00 26.78 ATOM 387 C VAL A 585 −9.049 10.41629.307 1.00 21.72 ATOM 388 O VAL A 585 −8.771 10.839 30.429 1.00 21.94ATOM 389 N GLN A 586 −10.291 10.118 28.945 1.00 22.79 ATOM 390 CA GLN A586 −11.394 10.290 29.881 1.00 25.11 ATOM 391 CB GLN A 586 −12.72810.306 29.131 1.00 34.29 ATOM 392 CG GLN A 586 −13.719 11.317 29.6781.00 39.65 ATOM 393 CD GLN A 586 −13.155 12.725 29.663 1.00 50.17 ATOM394 OE1 GLN A 586 −12.715 13.218 28.622 1.00 52.20 ATOM 395 NE2 GLN A586 −13.160 13.380 30.820 1.00 48.68 ATOM 396 C GLN A 586 −11.402 9.17230.914 1.00 22.36 ATOM 397 O GLN A 586 −11.587 9.413 32.108 1.00 23.81ATOM 398 N ASN A 587 −11.195 7.948 30.441 1.00 22.47 ATOM 399 CA ASN A587 −11.181 6.769 31.298 1.00 19.07 ATOM 400 CB ASN A 587 −10.651 5.56530.507 1.00 21.06 ATOM 401 CG ASN A 587 −10.944 4.236 31.179 1.00 29.14ATOM 402 OD1 ASN A 587 −11.098 4.157 32.397 1.00 21.26 ATOM 403 ND2 ASNA 587 −11.002 3.174 30.382 1.00 33.44 ATOM 404 C ASN A 587 −10.319 6.98132.542 1.00 20.86 ATOM 405 O ASN A 587 −10.727 6.646 33.656 1.00 19.43ATOM 406 N PHE A 588 −9.134 7.553 32.357 1.00 18.57 ATOM 407 CA PHE A588 −8.227 7.753 33.480 1.00 18.65 ATOM 408 CB PHE A 588 −6.880 7.10933.145 1.00 13.88 ATOM 409 CG PHE A 588 −6.976 5.624 32.948 1.00 14.75ATOM 410 CD1 PHE A 588 −7.272 4.791 34.022 1.00 13.58 ATOM 411 CD2 PHE A588 −6.860 5.065 31.686 1.00 12.05 ATOM 412 CE1 PHE A 588 −7.456 3.43133.837 1.00 13.16 ATOM 413 CE2 PHE A 588 −7.044 3.704 31.496 1.00 10.45ATOM 414 CZ PHE A 588 −7.344 2.888 32.576 1.00 16.21 ATOM 415 C PHE A588 −8.063 9.190 33.966 1.00 20.57 ATOM 416 O PHE A 588 −7.072 9.53834.611 1.00 18.90 ATOM 417 N GLN A 589 −9.052 10.020 33.662 1.00 21.41ATOM 418 CA GLN A 589 −9.057 11.410 34.110 1.00 23.36 ATOM 419 CB GLN A589 −9.213 11.449 35.634 1.00 28.73 ATOM 420 CG GLN A 589 −10.311 10.55136.194 1.00 40.43 ATOM 421 CD GLN A 589 −11.701 11.003 35.797 1.00 42.17ATOM 422 OE1 GLN A 589 −12.058 12.167 35.971 1.00 38.12 ATOM 423 NE2 GLNA 589 −12.498 10.080 35.270 1.00 47.35 ATOM 424 C GLN A 589 −7.80512.201 33.725 1.00 20.90 ATOM 425 O GLN A 589 −7.282 12.972 34.531 1.0021.16 ATOM 426 N MET A 590 −7.321 12.019 32.502 1.00 22.12 ATOM 427 CAMET A 590 −6.133 12.745 32.069 1.00 21.73 ATOM 428 CB MET A 590 −5.46312.035 30.893 1.00 22.93 ATOM 429 CG MET A 590 −4.751 10.752 31.257 1.0024.06 ATOM 430 SD MET A 590 −3.865 10.087 29.838 1.00 19.72 ATOM 431 CEMET A 590 −3.631 8.404 30.357 1.00 17.35 ATOM 432 C MET A 590 −6.45514.172 31.654 1.00 22.68 ATOM 433 O MET A 590 −7.295 14.398 30.784 1.0023.69 ATOM 434 N LYS A 591 −5.792 15.138 32.278 1.00 20.35 ATOM 435 CALYS A 591 −6.013 16.530 31.919 1.00 20.85 ATOM 436 CB LYS A 591 −5.55417.460 33.045 1.00 22.95 ATOM 437 CG LYS A 591 −6.472 17.422 34.262 1.0028.61 ATOM 438 CD LYS A 591 −6.065 18.438 35.315 1.00 37.59 ATOM 439 CELYS A 591 −7.106 18.527 36.423 1.00 42.92 ATOM 440 NZ LYS A 591 −8.41719.026 35.915 1.00 51.43 ATOM 441 C LYS A 591 −5.235 16.800 30.636 1.0020.72 ATOM 442 O LYS A 591 −4.048 16.486 30.537 1.00 21.29 ATOM 443 NHIS A 592 −5.920 17.375 29.654 1.00 20.84 ATOM 444 CA HIS A 592 −5.33317.670 28.351 1.00 21.11 ATOM 445 CB HIS A 592 −6.273 18.577 27.553 1.0021.39 ATOM 446 CG HIS A 592 −5.884 18.737 26.125 1.00 18.05 ATOM 447 CD2HIS A 592 −5.427 19.798 25.424 1.00 24.75 ATOM 448 ND1 HIS A 592 −5.92617.685 25.213 1.00 22.74 ATOM 449 CE1 HIS A 592 −5.518 18.102 24.0441.00 29.20 ATOM 450 NE2 HIS A 592 −5.204 19.393 24.135 1.00 27.94 ATOM451 C HIS A 592 −3.937 18.295 28.377 1.00 20.49 ATOM 452 O HIS A 592−3.034 17.848 27.661 1.00 19.49 ATOM 453 N GLU A 593 −3.765 19.33829.184 1.00 19.12 ATOM 454 CA GLU A 593 −2.481 20.019 29.279 1.00 18.26ATOM 455 CB GLU A 593 −2.592 21.243 30.192 1.00 23.02 ATOM 456 CG GLU A593 −1.267 21.957 30.416 1.00 32.52 ATOM 457 CD GLU A 593 −1.422 23.29631.116 1.00 44.01 ATOM 458 OE1 GLU A 593 −2.062 24.200 30.535 1.00 41.08ATOM 459 OE2 GLU A 593 −0.901 23.446 32.244 1.00 45.85 ATOM 460 C GLU A593 −1.381 19.099 29.793 1.00 18.42 ATOM 461 O GLU A 593 −0.230 19.19529.365 1.00 16.87 ATOM 462 N VAL A 594 −1.738 18.209 30.710 1.00 18.22ATOM 463 CA VAL A 594 −0.770 17.275 31.277 1.00 17.13 ATOM 464 CB VAL A594 −1.372 16.506 32.465 1.00 16.16 ATOM 465 CG1 VAL A 594 −0.314 15.60533.085 1.00 20.37 ATOM 466 CG2 VAL A 594 −1.911 17.481 33.491 1.00 22.54ATOM 467 C VAL A 594 −0.299 16.263 30.235 1.00 15.25 ATOM 468 O VAL A594 0.902 16.005 30.101 1.00 16.26 ATOM 469 N LEU A 595 −1.246 15.68129.504 1.00 13.83 ATOM 470 CA LEU A 595 −0.897 14.705 28.478 1.00 14.01ATOM 471 CB LEU A 595 −2.163 14.147 27.818 1.00 9.50 ATOM 472 CG LEU A595 −1.969 13.167 26.653 1.00 18.45 ATOM 473 CD1 LEU A 595 −1.068 12.01427.076 1.00 12.38 ATOM 474 CD2 LEU A 595 −3.318 12.643 26.201 1.00 14.12ATOM 475 C LEU A 595 −0.002 15.372 27.438 1.00 13.61 ATOM 476 O LEU A595 1.004 14.804 27.010 1.00 13.98 ATOM 477 N CYS A 596 −0.358 16.58827.037 1.00 14.70 ATOM 478 CA CYS A 596 0.448 17.303 26.058 1.00 12.24ATOM 479 CB CYS A 596 −0.191 18.649 25.709 1.00 15.21 ATOM 480 SG CYS A596 −1.702 18.507 24.749 1.00 17.45 ATOM 481 C CYS A 596 1.861 17.53426.586 1.00 12.70 ATOM 482 O CYS A 596 2.839 17.327 25.868 1.00 11.06ATOM 483 N ARG A 597 1.970 17.959 27.841 1.00 11.36 ATOM 484 CA ARG A597 3.283 18.211 28.420 1.00 11.51 ATOM 485 CB ARG A 597 3.141 18.83629.815 1.00 14.74 ATOM 486 CG ARG A 597 4.463 19.343 30.388 1.00 15.86ATOM 487 CD ARG A 597 4.294 20.067 31.727 1.00 20.22 ATOM 488 NE ARG A597 3.565 21.332 31.614 1.00 21.93 ATOM 489 CZ ARG A 597 2.279 21.49331.916 1.00 27.00 ATOM 490 NH1 ARG A 597 1.560 20.469 32.357 1.00 22.77ATOM 491 NH2 ARG A 597 1.708 22.683 31.782 1.00 30.27 ATOM 492 C ARG A597 4.100 16.919 28.494 1.00 11.80 ATOM 493 O ARG A 597 5.287 16.90928.162 1.00 10.48 ATOM 494 N TRP A 598 3.454 15.830 28.905 1.00 11.97ATOM 495 CA TRP A 598 4.112 14.530 29.022 1.00 9.62 ATOM 496 CB TRP A598 3.125 13.488 29.556 1.00 11.57 ATOM 497 CG TRP A 598 3.717 12.11029.702 1.00 10.65 ATOM 498 CD2 TRP A 598 3.609 11.028 28.771 1.00 9.66ATOM 499 CE2 TRP A 598 4.350 9.948 29.298 1.00 8.24 ATOM 500 CE3 TRP A598 2.964 10.866 27.541 1.00 11.87 ATOM 501 CD1 TRP A 598 4.494 11.65630.728 1.00 9.74 ATOM 502 NE1 TRP A 598 4.878 10.359 30.492 1.00 11.42ATOM 503 CZ2 TRP A 598 4.459 8.720 28.635 1.00 7.38 ATOM 504 CZ3 TRP A598 3.075 9.646 26.886 1.00 9.43 ATOM 505 CH2 TRP A 598 3.818 8.59327.434 1.00 10.02 ATOM 506 C TRP A 598 4.656 14.064 27.670 1.00 12.66ATOM 507 O TRP A 598 5.804 13.617 27.568 1.00 11.33 ATOM 508 N ILE A 5993.823 14.160 26.637 1.00 9.84 ATOM 509 CA ILE A 599 4.232 13.748 25.2981.00 12.03 ATOM 510 CB ILE A 599 3.101 13.974 24.270 1.00 11.30 ATOM 511CG2 ILE A 599 3.648 13.807 22.856 1.00 13.41 ATOM 512 CG1 ILE A 5991.953 13.000 24.546 1.00 13.16 ATOM 513 CD1 ILE A 599 0.732 13.21823.668 1.00 13.06 ATOM 514 C ILE A 599 5.460 14.533 24.855 1.00 14.21ATOM 515 O ILE A 599 6.414 13.969 24.308 1.00 11.47 ATOM 516 N LEU A 6005.439 15.839 25.094 1.00 14.33 ATOM 517 CA LEU A 600 6.566 16.670 24.7071.00 13.61 ATOM 518 CB LEU A 600 6.214 18.151 24.882 1.00 13.53 ATOM 519CG LEU A 600 5.073 18.621 23.971 1.00 12.80 ATOM 520 CD1 LEU A 600 4.65220.036 24.336 1.00 15.66 ATOM 521 CD2 LEU A 600 5.518 18.557 22.520 1.0013.09 ATOM 522 C LEU A 600 7.800 16.297 25.523 1.00 10.78 ATOM 523 O LEUA 600 8.917 16.324 25.011 1.00 10.47 ATOM 524 N SER A 601 7.601 15.92526.788 1.00 10.50 ATOM 525 CA SER A 601 8.734 15.540 27.624 1.00 8.54ATOM 526 CB SER A 601 8.303 15.398 29.085 1.00 9.00 ATOM 527 OG SER A601 8.036 16.678 29.634 1.00 9.87 ATOM 528 C SER A 601 9.342 14.23927.129 1.00 9.99 ATOM 529 O SER A 601 10.563 14.082 27.104 1.00 10.43ATOM 530 N VAL A 602 8.487 13.300 26.739 1.00 10.77 ATOM 531 CA VAL A602 8.968 12.024 26.223 1.00 10.98 ATOM 532 CB VAL A 602 7.791 11.08125.874 1.00 12.52 ATOM 533 CG1 VAL A 602 8.303 9.856 25.138 1.00 9.22ATOM 534 CG2 VAL A 602 7.068 10.658 27.152 1.00 11.71 ATOM 535 C VAL A602 9.794 12.290 24.967 1.00 12.57 ATOM 536 O VAL A 602 10.935 11.84824.855 1.00 11.99 ATOM 537 N LYS A 603 9.220 13.043 24.034 1.00 12.97ATOM 538 CA LYS A 603 9.906 13.363 22.792 1.00 11.73 ATOM 539 CB LYS A603 9.025 14.268 21.928 1.00 14.00 ATOM 540 CG LYS A 603 9.666 14.68820.620 1.00 14.56 ATOM 541 CD LYS A 603 8.656 15.317 19.686 1.00 16.82ATOM 542 CE LYS A 603 8.088 16.603 20.262 1.00 24.97 ATOM 543 NZ LYS A603 7.169 17.256 19.300 1.00 39.23 ATOM 544 C LYS A 603 11.256 14.03523.042 1.00 11.50 ATOM 545 O LYS A 603 12.252 13.694 22.414 1.00 14.04ATOM 546 N LYS A 604 11.279 14.985 23.968 1.00 11.12 ATOM 547 CA LYS A604 12.501 15.714 24.293 1.00 13.84 ATOM 548 CB LYS A 604 12.181 16.84925.274 1.00 16.59 ATOM 549 CG LYS A 604 13.403 17.589 25.788 1.00 18.98ATOM 550 CD LYS A 604 13.016 18.673 26.784 1.00 25.53 ATOM 551 CE LYS A604 14.251 19.335 27.391 1.00 31.51 ATOM 552 NZ LYS A 604 13.893 20.35128.424 1.00 29.80 ATOM 553 C LYS A 604 13.582 14.824 24.890 1.00 12.98ATOM 554 O LYS A 604 14.776 15.073 24.710 1.00 13.10 ATOM 555 N ASN A605 13.173 13.773 25.587 1.00 12.62 ATOM 556 CA ASN A 605 14.146 12.90126.220 1.00 13.04 ATOM 557 CB ASN A 605 13.555 12.336 27.507 1.00 13.13ATOM 558 CG ASN A 605 13.579 13.356 28.638 1.00 32.58 ATOM 559 OD1 ASN A605 14.638 13.650 29.197 1.00 25.76 ATOM 560 ND2 ASN A 605 12.418 13.91828.962 1.00 30.95 ATOM 561 C ASN A 605 14.757 11.809 25.352 1.00 15.12ATOM 562 O ASN A 605 15.342 10.848 25.858 1.00 18.48 ATOM 563 N TYR A606 14.612 11.961 24.042 1.00 10.60 ATOM 564 CA TYR A 606 15.233 11.05123.093 1.00 10.45 ATOM 565 CB TYR A 606 14.254 10.645 21.982 1.00 10.34ATOM 566 CG TYR A 606 13.420 9.444 22.358 1.00 11.02 ATOM 567 CD1 TYR A606 13.950 8.156 22.297 1.00 8.31 ATOM 568 CE1 TYR A 606 13.222 7.06122.752 1.00 8.28 ATOM 569 CD2 TYR A 606 12.139 9.601 22.874 1.00 12.47ATOM 570 CE2 TYR A 606 11.410 8.516 23.335 1.00 15.05 ATOM 571 CZ TYR A606 11.955 7.252 23.275 1.00 15.46 ATOM 572 OH TYR A 606 11.227 6.18823.773 1.00 12.36 ATOM 573 C TYR A 606 16.362 11.908 22.539 1.00 11.41ATOM 574 O TYR A 606 16.216 13.129 22.428 1.00 14.91 ATOM 575 N ARG A607 17.499 11.293 22.234 1.00 11.41 ATOM 576 CA ARG A 607 18.627 12.04221.700 1.00 10.90 ATOM 577 CB ARG A 607 19.933 11.322 22.034 1.00 12.68ATOM 578 CG ARG A 607 20.078 11.019 23.520 1.00 10.36 ATOM 579 CD ARG A607 21.460 10.489 23.870 1.00 13.25 ATOM 580 NE ARG A 607 21.492 9.92925.221 1.00 9.55 ATOM 581 CZ ARG A 607 22.601 9.556 25.854 1.00 18.33ATOM 582 NH1 ARG A 607 23.781 9.686 25.262 1.00 13.50 ATOM 583 NH2 ARG A607 22.530 9.045 27.077 1.00 17.68 ATOM 584 C ARG A 607 18.425 12.15020.194 1.00 10.45 ATOM 585 O ARG A 607 18.616 11.182 19.458 1.00 12.53ATOM 586 N LYS A 608 18.052 13.340 19.738 1.00 11.88 ATOM 587 CA LYS A608 17.755 13.555 18.323 1.00 13.33 ATOM 588 CB LYS A 608 17.273 14.99318.104 1.00 18.33 ATOM 589 CG LYS A 608 18.226 16.064 18.574 1.00 34.41ATOM 590 CD LYS A 608 17.558 17.429 18.538 1.00 39.16 ATOM 591 CE LYS A608 18.430 18.485 19.193 1.00 44.56 ATOM 592 NZ LYS A 608 19.755 18.59518.525 1.00 49.34 ATOM 593 C LYS A 608 18.837 13.220 17.311 1.00 13.41ATOM 594 O LYS A 608 18.527 12.904 16.164 1.00 14.71 ATOM 595 N ASN A609 20.098 13.272 17.724 1.00 12.65 ATOM 596 CA ASN A 609 21.185 12.97716.804 1.00 15.37 ATOM 597 CB ASN A 609 22.383 13.872 17.121 1.00 19.55ATOM 598 CG ASN A 609 22.059 15.347 16.952 1.00 21.29 ATOM 599 OD1 ASN A609 21.630 15.779 15.882 1.00 28.72 ATOM 600 ND2 ASN A 609 22.261 16.12618.009 1.00 36.76 ATOM 601 C ASN A 609 21.593 11.507 16.743 1.00 14.47ATOM 602 O ASN A 609 22.486 11.135 15.981 1.00 15.29 ATOM 603 N VAL A610 20.955 10.670 17.557 1.00 11.89 ATOM 604 CA VAL A 610 21.221 9.23317.511 1.00 11.43 ATOM 605 CB VAL A 610 20.696 8.531 18.777 1.00 11.38ATOM 606 CG1 VAL A 610 20.649 7.019 18.571 1.00 10.56 ATOM 607 CG2 VAL A610 21.608 8.882 19.955 1.00 10.47 ATOM 608 C VAL A 610 20.432 8.80916.272 1.00 12.97 ATOM 609 O VAL A 610 19.221 9.025 16.198 1.00 11.59ATOM 610 N ALA A 611 21.131 8.223 15.302 1.00 11.37 ATOM 611 CA ALA A611 20.554 7.833 14.018 1.00 12.77 ATOM 612 CB ALA A 611 21.579 7.02113.223 1.00 12.83 ATOM 613 C ALA A 611 19.208 7.117 13.981 1.00 12.88ATOM 614 O ALA A 611 18.305 7.522 13.247 1.00 14.79 ATOM 615 N TYR A 61219.071 6.050 14.756 1.00 12.18 ATOM 616 CA TYR A 612 17.830 5.288 14.7431.00 10.69 ATOM 617 CB TYR A 612 18.147 3.824 14.408 1.00 13.15 ATOM 618CG TYR A 612 16.968 2.877 14.509 1.00 12.63 ATOM 619 CD1 TYR A 61215.832 3.054 13.729 1.00 19.45 ATOM 620 CE1 TYR A 612 14.752 2.18513.833 1.00 24.00 ATOM 621 CD2 TYR A 612 16.996 1.805 15.392 1.00 13.47ATOM 622 CE2 TYR A 612 15.930 0.938 15.503 1.00 24.95 ATOM 623 CZ TYR A612 14.812 1.129 14.722 1.00 24.27 ATOM 624 OH TYR A 612 13.761 0.24514.831 1.00 25.94 ATOM 625 C TYR A 612 17.017 5.371 16.028 1.00 11.05ATOM 626 O TYR A 612 15.812 5.632 15.989 1.00 9.25 ATOM 627 N HIS A 61317.667 5.159 17.166 1.00 10.71 ATOM 628 CA HIS A 613 16.951 5.199 18.4321.00 9.46 ATOM 629 CB HIS A 613 17.694 4.391 19.499 1.00 12.29 ATOM 630CG HIS A 613 17.706 2.923 19.232 1.00 13.22 ATOM 631 CD2 HIS A 61316.742 1.983 19.364 1.00 13.53 ATOM 632 ND1 HIS A 613 18.811 2.26218.726 1.00 8.83 ATOM 633 CE1 HIS A 613 18.523 0.989 18.562 1.00 12.86ATOM 634 NE2 HIS A 613 17.268 0.789 18.942 1.00 16.65 ATOM 635 C HIS A613 16.686 6.606 18.936 1.00 11.81 ATOM 636 O HIS A 613 17.226 7.02319.957 1.00 11.26 ATOM 637 N ASN A 614 15.859 7.333 18.192 1.00 12.20ATOM 638 CA ASN A 614 15.459 8.685 18.556 1.00 11.65 ATOM 639 CB ASN A614 15.955 9.702 17.516 1.00 19.08 ATOM 640 CG ASN A 614 15.631 9.29516.090 1.00 17.63 ATOM 641 OD1 ASN A 614 16.529 9.151 15.253 1.00 16.40ATOM 642 ND2 ASN A 614 14.349 9.115 15.802 1.00 11.39 ATOM 643 C ASN A614 13.933 8.690 18.644 1.00 11.53 ATOM 644 O ASN A 614 13.298 7.64718.493 1.00 9.32 ATOM 645 N TRP A 615 13.342 9.850 18.890 1.00 8.95 ATOM646 CA TRP A 615 11.893 9.929 19.015 1.00 9.02 ATOM 647 CB TRP A 61511.457 11.397 19.127 1.00 9.00 ATOM 648 CG TRP A 615 10.002 11.63818.809 1.00 8.75 ATOM 649 CD2 TRP A 615 8.860 11.228 19.581 1.00 10.58ATOM 650 CE2 TRP A 615 7.709 11.655 18.883 1.00 12.68 ATOM 651 CE3 TRP A615 8.698 10.542 20.789 1.00 12.70 ATOM 652 CD1 TRP A 615 9.504 12.27917.709 1.00 11.21 ATOM 653 NE1 TRP A 615 8.132 12.292 17.747 1.00 11.25ATOM 654 CZ2 TRP A 615 6.414 11.418 19.354 1.00 12.28 ATOM 655 CZ3 TRP A615 7.410 10.307 21.255 1.00 18.15 ATOM 656 CH2 TRP A 615 6.286 10.74420.536 1.00 13.05 ATOM 657 C TRP A 615 11.090 9.237 17.910 1.00 8.08ATOM 658 O TRP A 615 10.093 8.579 18.197 1.00 9.24 ATOM 659 N ARG A 61611.514 9.365 16.656 1.00 9.61 ATOM 660 CA ARG A 616 10.750 8.759 15.5701.00 11.24 ATOM 661 CB ARG A 616 11.346 9.129 14.206 1.00 9.33 ATOM 662CG ARG A 616 11.241 10.630 13.885 1.00 13.33 ATOM 663 CD ARG A 616 9.81711.169 14.120 1.00 11.22 ATOM 664 NE ARG A 616 9.705 12.598 13.823 1.0013.61 ATOM 665 CZ ARG A 616 9.119 13.103 12.741 1.00 15.86 ATOM 666 NH1ARG A 616 8.577 12.300 11.834 1.00 15.89 ATOM 667 NH2 ARG A 616 9.07314.419 12.564 1.00 19.53 ATOM 668 C ARG A 616 10.607 7.250 15.705 1.009.88 ATOM 669 O ARG A 616 9.575 6.692 15.328 1.00 10.40 ATOM 670 N HIS A617 11.625 6.582 16.242 1.00 7.87 ATOM 671 CA HIS A 617 11.514 5.14116.419 1.00 7.37 ATOM 672 CB HIS A 617 12.862 4.523 16.782 1.00 11.98ATOM 673 CG HIS A 617 12.742 3.163 17.390 1.00 8.70 ATOM 674 CD2 HIS A617 13.043 2.715 18.632 1.00 9.51 ATOM 675 ND1 HIS A 617 12.206 2.08816.713 1.00 8.99 ATOM 676 CE1 HIS A 617 12.183 1.036 17.510 1.00 11.83ATOM 677 NE2 HIS A 617 12.684 1.391 18.681 1.00 10.58 ATOM 678 C HIS A617 10.488 4.816 17.506 1.00 8.63 ATOM 679 O HIS A 617 9.692 3.88817.361 1.00 10.24 ATOM 680 N ALA A 618 10.498 5.586 18.591 1.00 7.45ATOM 681 CA ALA A 618 9.549 5.358 19.687 1.00 8.54 ATOM 682 CB ALA A 6189.887 6.261 20.864 1.00 11.31 ATOM 683 C ALA A 618 8.126 5.637 19.2101.00 8.39 ATOM 684 O ALA A 618 7.184 4.900 19.523 1.00 9.03 ATOM 685 NPHE A 619 7.981 6.725 18.465 1.00 8.88 ATOM 686 CA PHE A 619 6.695 7.11817.911 1.00 9.63 ATOM 687 CB PHE A 619 6.850 8.418 17.119 1.00 12.92ATOM 688 CG PHE A 619 5.618 8.809 16.357 1.00 10.44 ATOM 689 CD1 PHE A619 4.432 9.066 17.021 1.00 18.21 ATOM 690 CD2 PHE A 619 5.646 8.91414.974 1.00 12.41 ATOM 691 CE1 PHE A 619 3.291 9.412 16.324 1.00 14.74ATOM 692 CE2 PHE A 619 4.508 9.260 14.270 1.00 13.16 ATOM 693 CZ PHE A619 3.328 9.512 14.947 1.00 11.01 ATOM 694 C PHE A 619 6.150 6.01716.996 1.00 9.52 ATOM 695 O PHE A 619 4.975 5.654 17.079 1.00 9.30 ATOM696 N ASN A 620 7.001 5.490 16.119 1.00 10.15 ATOM 697 CA ASN A 6206.583 4.428 15.204 1.00 11.34 ATOM 698 CB ASN A 620 7.694 4.123 14.1941.00 9.10 ATOM 699 CG ASN A 620 7.658 5.052 12.999 1.00 17.16 ATOM 700OD1 ASN A 620 8.665 5.656 12.634 1.00 19.51 ATOM 701 ND2 ASN A 620 6.4905.166 12.382 1.00 12.88 ATOM 702 C ASN A 620 6.206 3.161 15.956 1.009.23 ATOM 703 O ASN A 620 5.273 2.457 15.574 1.00 10.76 ATOM 704 N THR A621 6.936 2.871 17.026 1.00 8.56 ATOM 705 CA THR A 621 6.650 1.68817.819 1.00 9.52 ATOM 706 CB THR A 621 7.707 1.509 18.928 1.00 8.96 ATOM707 OG1 THR A 621 9.010 1.404 18.328 1.00 9.14 ATOM 708 CG2 THR A 6217.428 0.244 19.736 1.00 7.93 ATOM 709 C THR A 621 5.252 1.821 18.4251.00 10.48 ATOM 710 O THR A 621 4.455 0.879 18.382 1.00 10.11 ATOM 711 NALA A 622 4.954 2.995 18.978 1.00 8.32 ATOM 712 CA ALA A 622 3.644 3.24419.573 1.00 9.28 ATOM 713 CB ALA A 622 3.642 4.583 20.294 1.00 9.90 ATOM714 C ALA A 622 2.567 3.224 18.488 1.00 10.02 ATOM 715 O ALA A 622 1.4472.769 18.721 1.00 8.06 ATOM 716 N GLN A 623 2.902 3.708 17.297 1.00 7.82ATOM 717 CA GLN A 623 1.927 3.708 16.211 1.00 10.17 ATOM 718 CB GLN A623 2.456 4.487 15.003 1.00 8.39 ATOM 719 CG GLN A 623 1.473 4.57813.825 1.00 8.23 ATOM 720 CD GLN A 623 1.444 3.319 12.967 1.00 13.63ATOM 721 OE1 GLN A 623 2.484 2.730 12.682 1.00 12.75 ATOM 722 NE2 GLN A623 0.258 2.919 12.535 1.00 11.69 ATOM 723 C GLN A 623 1.597 2.27815.806 1.00 10.35 ATOM 724 O GLN A 623 0.449 1.962 15.501 1.00 9.61 ATOM725 N CYS A 624 2.601 1.406 15.802 1.00 9.08 ATOM 726 CA CYS A 624 2.3550.017 15.439 1.00 9.34 ATOM 727 CB CYS A 624 3.679 −0.740 15.273 1.0011.00 ATOM 728 SG CYS A 624 3.481 −2.446 14.713 1.00 11.71 ATOM 729 CCYS A 624 1.495 −0.625 16.529 1.00 10.17 ATOM 730 O CYS A 624 0.631−1.448 16.239 1.00 10.64 ATOM 731 N MET A 625 1.728 −0.238 17.781 1.009.06 ATOM 732 CA MET A 625 0.933 −0.764 18.892 1.00 9.38 ATOM 733 CB META 625 1.418 −0.180 20.225 1.00 8.21 ATOM 734 CG MET A 625 0.692 −0.71821.466 1.00 8.16 ATOM 735 SD MET A 625 0.904 −2.512 21.728 1.00 11.88ATOM 736 CE MET A 625 2.600 −2.586 22.309 1.00 11.24 ATOM 737 C MET A625 −0.529 −0.376 18.661 1.00 9.31 ATOM 738 O MET A 625 −1.434 −1.20818.757 1.00 10.06 ATOM 739 N PHE A 626 −0.757 0.896 18.353 1.00 9.47ATOM 740 CA PHE A 626 −2.112 1.377 18.092 1.00 9.60 ATOM 741 CB PHE A626 −2.077 2.859 17.725 1.00 9.70 ATOM 742 CG PHE A 626 −3.432 3.45117.461 1.00 7.25 ATOM 743 CD1 PHE A 626 −4.241 3.858 18.509 1.00 13.86ATOM 744 CD2 PHE A 626 −3.897 3.598 16.163 1.00 13.47 ATOM 745 CE1 PHE A626 −5.491 4.411 18.267 1.00 18.88 ATOM 746 CE2 PHE A 626 −5.144 4.14715.917 1.00 11.81 ATOM 747 CZ PHE A 626 −5.942 4.552 16.970 1.00 16.53ATOM 748 C PHE A 626 −2.737 0.579 16.940 1.00 10.98 ATOM 749 O PHE A 626−3.862 0.084 17.047 1.00 12.71 ATOM 750 N ALA A 627 −1.999 0.455 15.8381.00 7.24 ATOM 751 CA ALA A 627 −2.486 −0.279 14.675 1.00 9.31 ATOM 752CB ALA A 627 −1.454 −0.220 13.549 1.00 14.42 ATOM 753 C ALA A 627 −2.803−1.734 15.024 1.00 11.79 ATOM 754 O ALA A 627 −3.815 −2.276 14.583 1.0011.59 ATOM 755 N ALA A 628 −1.945 −2.361 15.824 1.00 10.63 ATOM 756 CAALA A 628 −2.158 −3.749 16.219 1.00 11.00 ATOM 757 CB ALA A 628 −0.934−4.280 16.961 1.00 11.43 ATOM 758 C ALA A 628 −3.398 −3.877 17.099 1.0011.16 ATOM 759 O ALA A 628 −4.152 −4.845 16.994 1.00 12.30 ATOM 760 NLEU A 629 −3.608 −2.896 17.970 1.00 9.63 ATOM 761 CA LEU A 629 −4.765−2.924 18.856 1.00 9.96 ATOM 762 CB LEU A 629 −4.627 −1.858 19.945 1.0012.79 ATOM 763 CG LEU A 629 −3.538 −2.115 20.990 1.00 10.87 ATOM 764 CD1LEU A 629 −3.286 −0.859 21.792 1.00 11.38 ATOM 765 CD2 LEU A 629 −3.956−3.264 21.897 1.00 14.99 ATOM 766 C LEU A 629 −6.051 −2.692 18.073 1.0012.31 ATOM 767 O LEU A 629 −7.084 −3.300 18.364 1.00 11.63 ATOM 768 NLYS A 630 −5.973 −1.822 17.070 1.00 11.64 ATOM 769 CA LYS A 630 −7.125−1.479 16.242 1.00 12.87 ATOM 770 CB LYS A 630 −6.984 −0.037 15.738 1.0015.53 ATOM 771 CG LYS A 630 −7.084 1.030 16.820 1.00 13.30 ATOM 772 CDLYS A 630 −8.495 1.104 17.385 1.00 19.60 ATOM 773 CE LYS A 630 −8.6982.349 18.245 1.00 18.93 ATOM 774 NZ LYS A 630 −7.877 2.334 19.481 1.0040.94 ATOM 775 C LYS A 630 −7.323 −2.422 15.049 1.00 13.54 ATOM 776 OLYS A 630 −8.122 −3.350 15.107 1.00 12.81 ATOM 777 N ALA A 631 −6.597−2.170 13.967 1.00 13.05 ATOM 778 CA ALA A 631 −6.701 −2.997 12.770 1.0014.94 ATOM 779 CB ALA A 631 −5.763 −2.460 11.688 1.00 17.58 ATOM 780 CALA A 631 −6.374 −4.461 13.068 1.00 16.22 ATOM 781 O ALA A 631 −6.960−5.375 12.479 1.00 15.44 ATOM 782 N GLY A 632 −5.439 −4.670 13.990 1.0012.88 ATOM 783 CA GLY A 632 −5.028 −6.014 14.359 1.00 13.10 ATOM 784 CGLY A 632 −5.995 −6.711 15.298 1.00 13.12 ATOM 785 O GLY A 632 −5.850−7.902 15.576 1.00 15.03 ATOM 786 N LYS A 633 −6.968 −5.959 15.803 1.0013.75 ATOM 787 CA LYS A 633 −7.997 −6.497 16.692 1.00 14.20 ATOM 788 CBLYS A 633 −8.815 −7.566 15.954 1.00 13.72 ATOM 789 CG LYS A 633 −9.438−7.109 14.631 1.00 23.64 ATOM 790 CD LYS A 633 −10.532 −6.072 14.8341.00 30.20 ATOM 791 CE LYS A 633 −11.182 −5.672 13.510 1.00 34.87 ATOM792 NZ LYS A 633 −10.227 −4.989 12.594 1.00 46.21 ATOM 793 C LYS A 633−7.464 −7.085 17.997 1.00 14.18 ATOM 794 O LYS A 633 −8.048 −8.02418.540 1.00 14.72 ATOM 795 N ILE A 634 −6.366 −6.536 18.507 1.00 13.07ATOM 796 CA ILE A 634 −5.801 −7.037 19.755 1.00 12.44 ATOM 797 CB ILE A634 −4.262 −6.819 19.799 1.00 13.52 ATOM 798 CG2 ILE A 634 −3.709 −7.23621.156 1.00 14.73 ATOM 799 CG1 ILE A 634 −3.581 −7.632 18.694 1.00 14.10ATOM 800 CD1 ILE A 634 −3.757 −9.128 18.829 1.00 14.44 ATOM 801 C ILE A634 −6.439 −6.346 20.967 1.00 12.23 ATOM 802 O ILE A 634 −6.456 −6.89422.067 1.00 12.06 ATOM 803 N GLN A 635 −6.990 −5.155 20.752 1.00 13.17ATOM 804 CA GLN A 635 −7.597 −4.377 21.834 1.00 12.59 ATOM 805 CB GLN A635 −8.330 −3.158 21.267 1.00 14.77 ATOM 806 CG GLN A 635 −8.796 −2.18022.345 1.00 17.07 ATOM 807 CD GLN A 635 −9.479 −0.949 21.778 1.00 17.87ATOM 808 OE1 GLN A 635 −9.080 −0.425 20.741 1.00 15.93 ATOM 809 NE2 GLNA 635 −10.509 −0.473 22.471 1.00 27.59 ATOM 810 C GLN A 635 −8.549−5.127 22.762 1.00 13.46 ATOM 811 O GLN A 635 −8.382 −5.107 23.984 1.0012.66 ATOM 812 N ASN A 636 −9.554 −5.778 22.188 1.00 12.36 ATOM 813 CAASN A 636 −10.533 −6.493 22.996 1.00 15.16 ATOM 814 CB ASN A 636 −11.736−6.872 22.130 1.00 13.54 ATOM 815 CG ASN A 636 −12.508 −5.655 21.6581.00 19.96 ATOM 816 OD1 ASN A 636 −12.211 −4.526 22.059 1.00 19.43 ATOM817 ND2 ASN A 636 −13.506 −5.874 20.810 1.00 20.88 ATOM 818 C ASN A 636−10.002 −7.708 23.743 1.00 14.39 ATOM 819 O ASN A 636 −10.720 −8.31224.539 1.00 17.61 ATOM 820 N LYS A 637 −8.744 −8.060 23.500 1.00 13.69ATOM 821 CA LYS A 637 −8.132 −9.194 24.180 1.00 13.94 ATOM 822 CB LYS A637 −7.124 −9.893 23.262 1.00 13.19 ATOM 823 CG LYS A 637 −7.667 −10.32821.910 1.00 16.41 ATOM 824 CD LYS A 637 −6.599 −11.079 21.128 1.00 18.79ATOM 825 CE LYS A 637 −7.110 −11.542 19.773 1.00 21.00 ATOM 826 NZ LYS A637 −8.266 −12.467 19.893 1.00 27.72 ATOM 827 C LYS A 637 −7.400 −8.70825.435 1.00 14.29 ATOM 828 O LYS A 637 −6.930 −9.514 26.237 1.00 15.91ATOM 829 N LEU A 638 −7.316 −7.391 25.611 1.00 13.88 ATOM 830 CA LEU A638 −6.602 −6.828 26.757 1.00 14.02 ATOM 831 CB LEU A 638 −5.426 −5.98826.256 1.00 14.42 ATOM 832 CG LEU A 638 −4.496 −6.595 25.201 1.00 13.65ATOM 833 CD1 LEU A 638 −3.405 −5.589 24.860 1.00 13.98 ATOM 834 CD2 LEUA 638 −3.881 −7.885 25.718 1.00 12.70 ATOM 835 C LEU A 638 −7.464 −5.97327.687 1.00 13.83 ATOM 836 O LEU A 638 −8.551 −5.529 27.313 1.00 16.24ATOM 837 N THR A 639 −6.968 −5.745 28.902 1.00 13.04 ATOM 838 CA THR A639 −7.665 −4.913 29.885 1.00 12.97 ATOM 839 CB THR A 639 −7.225 −5.24431.323 1.00 9.72 ATOM 840 OG1 THR A 639 −5.883 −4.777 31.534 1.00 11.58ATOM 841 CG2 THR A 639 −7.284 −6.752 31.574 1.00 13.01 ATOM 842 C THR A639 −7.320 −3.443 29.627 1.00 11.14 ATOM 843 O THR A 639 −6.369 −3.14728.910 1.00 12.39 ATOM 844 N ASP A 640 −8.082 −2.524 30.216 1.00 11.83ATOM 845 CA ASP A 640 −7.814 −1.098 30.027 1.00 11.03 ATOM 846 CB ASP A640 −8.846 −0.243 30.774 1.00 9.58 ATOM 847 CG ASP A 640 −10.238 −0.36830.191 1.00 23.27 ATOM 848 OD1 ASP A 640 −10.357 −0.828 29.037 1.0021.74 ATOM 849 OD2 ASP A 640 −11.211 0.011 30.879 1.00 18.96 ATOM 850 CASP A 640 −6.419 −0.724 30.519 1.00 10.85 ATOM 851 O ASP A 640 −5.7080.058 29.881 1.00 11.05 ATOM 852 N LEU A 641 −6.031 −1.290 31.655 1.0011.16 ATOM 853 CA LEU A 641 −4.727 −1.004 32.235 1.00 10.51 ATOM 854 CBLEU A 641 −4.628 −1.606 33.640 1.00 13.05 ATOM 855 CG LEU A 641 −5.633−1.081 34.674 1.00 13.28 ATOM 856 CD1 LEU A 641 −5.383 −1.762 36.0051.00 14.91 ATOM 857 CD2 LEU A 641 −5.506 0.432 34.813 1.00 12.98 ATOM858 C LEU A 641 −3.593 −1.527 31.359 1.00 10.02 ATOM 859 O LEU A 641−2.550 −0.883 31.237 1.00 9.79 ATOM 860 N GLU A 642 −3.791 −2.692 30.7481.00 9.49 ATOM 861 CA GLU A 642 −2.756 −3.253 29.886 1.00 9.55 ATOM 862CB GLU A 642 −3.120 −4.687 29.493 1.00 13.24 ATOM 863 CG GLU A 642−3.215 −5.605 30.705 1.00 17.56 ATOM 864 CD GLU A 642 −3.645 −7.02130.373 1.00 14.47 ATOM 865 OE1 GLU A 642 −4.411 −7.212 29.404 1.00 12.63ATOM 866 OE2 GLU A 642 −3.233 −7.949 31.108 1.00 15.36 ATOM 867 C GLU A642 −2.568 −2.366 28.656 1.00 9.56 ATOM 868 O GLU A 642 −1.442 −2.13528.217 1.00 10.36 ATOM 869 N ILE A 643 −3.665 −1.847 28.112 1.00 9.98ATOM 870 CA ILE A 643 −3.585 −0.978 26.945 1.00 11.53 ATOM 871 CB ILE A643 −4.992 −0.683 26.391 1.00 12.52 ATOM 872 CG2 ILE A 643 −4.915 0.36725.281 1.00 11.83 ATOM 873 CG1 ILE A 643 −5.614 −1.984 25.885 1.00 11.82ATOM 874 CD1 ILE A 643 −7.089 −1.872 25.553 1.00 18.49 ATOM 875 C ILE A643 −2.883 0.323 27.339 1.00 9.56 ATOM 876 O ILE A 643 −1.993 0.80626.635 1.00 10.76 ATOM 877 N LEU A 644 −3.278 0.880 28.479 1.00 9.68ATOM 878 CA LEU A 644 −2.663 2.105 28.974 1.00 9.78 ATOM 879 CB LEU A644 −3.285 2.482 30.321 1.00 11.15 ATOM 880 CG LEU A 644 −2.658 3.64331.093 1.00 14.02 ATOM 881 CD1 LEU A 644 −2.853 4.946 30.328 1.00 14.15ATOM 882 CD2 LEU A 644 −3.315 3.735 32.471 1.00 14.10 ATOM 883 C LEU A644 −1.152 1.899 29.139 1.00 9.98 ATOM 884 O LEU A 644 −0.342 2.72028.694 1.00 9.97 ATOM 885 N ALA A 645 −0.778 0.788 29.766 1.00 8.98 ATOM886 CA ALA A 645 0.634 0.492 30.008 1.00 8.84 ATOM 887 CB ALA A 6450.763 −0.724 30.928 1.00 8.17 ATOM 888 C ALA A 645 1.414 0.256 28.7181.00 9.39 ATOM 889 O ALA A 645 2.556 0.687 28.598 1.00 9.92 ATOM 890 NLEU A 646 0.799 −0.430 27.761 1.00 8.76 ATOM 891 CA LEU A 646 1.462−0.708 26.488 1.00 8.34 ATOM 892 CB LEU A 646 0.607 −1.652 25.644 1.0010.30 ATOM 893 CG LEU A 646 0.541 −3.101 26.128 1.00 11.47 ATOM 894 CD1LEU A 646 −0.557 −3.832 25.379 1.00 15.28 ATOM 895 CD2 LEU A 646 1.879−3.779 25.906 1.00 10.48 ATOM 896 C LEU A 646 1.761 0.550 25.682 1.007.55 ATOM 897 O LEU A 646 2.837 0.676 25.094 1.00 9.05 ATOM 898 N LEU A647 0.812 1.479 25.643 1.00 7.57 ATOM 899 CA LEU A 647 1.020 2.71324.889 1.00 8.87 ATOM 900 CB LEU A 647 −0.283 3.516 24.803 1.00 7.82ATOM 901 CG LEU A 647 −0.214 4.722 23.862 1.00 10.06 ATOM 902 CD1 LEU A647 0.194 4.251 22.470 1.00 13.81 ATOM 903 CD2 LEU A 647 −1.560 5.43723.820 1.00 12.05 ATOM 904 C LEU A 647 2.120 3.550 25.540 1.00 8.12 ATOM905 O LEU A 647 3.011 4.070 24.863 1.00 8.78 ATOM 906 N ILE A 648 2.0563.676 26.860 1.00 9.66 ATOM 907 CA ILE A 648 3.065 4.429 27.597 1.008.86 ATOM 908 CB ILE A 648 2.692 4.501 29.100 1.00 10.81 ATOM 909 CG2ILE A 648 3.851 5.063 29.917 1.00 7.70 ATOM 910 CG1 ILE A 648 1.4395.364 29.266 1.00 11.45 ATOM 911 CD1 ILE A 648 0.921 5.437 30.688 1.009.57 ATOM 912 C ILE A 648 4.427 3.756 27.424 1.00 8.38 ATOM 913 O ILE A648 5.439 4.427 27.180 1.00 9.63 ATOM 914 N ALA A 649 4.456 2.430 27.5361.00 9.32 ATOM 915 CA ALA A 649 5.710 1.697 27.388 1.00 9.98 ATOM 916 CBALA A 649 5.506 0.214 27.703 1.00 11.64 ATOM 917 C ALA A 649 6.285 1.85325.989 1.00 9.64 ATOM 918 O ALA A 649 7.471 2.126 25.831 1.00 10.34 ATOM919 N ALA A 650 5.449 1.680 24.971 1.00 11.02 ATOM 920 CA ALA A 6505.914 1.814 23.591 1.00 9.43 ATOM 921 CB ALA A 650 4.747 1.618 22.6171.00 8.79 ATOM 922 C ALA A 650 6.561 3.183 23.359 1.00 8.11 ATOM 923 OALA A 650 7.628 3.292 22.748 1.00 9.60 ATOM 924 N LEU A 651 5.914 4.23323.851 1.00 9.58 ATOM 925 CA LEU A 651 6.443 5.582 23.679 1.00 10.27ATOM 926 CB LEU A 651 5.383 6.613 24.066 1.00 9.84 ATOM 927 CG LEU A 6514.198 6.717 23.101 1.00 6.24 ATOM 928 CD1 LEU A 651 3.038 7.432 23.7721.00 14.57 ATOM 929 CD2 LEU A 651 4.637 7.463 21.846 1.00 11.43 ATOM 930C LEU A 651 7.706 5.848 24.488 1.00 10.46 ATOM 931 O LEU A 651 8.5736.611 24.066 1.00 9.75 ATOM 932 N SER A 652 7.807 5.194 25.640 1.00 9.58ATOM 933 CA SER A 652 8.935 5.394 26.542 1.00 10.30 ATOM 934 CB SER A652 8.422 5.453 27.983 1.00 9.30 ATOM 935 OG SER A 652 7.367 6.37928.133 1.00 11.78 ATOM 936 C SER A 652 10.026 4.334 26.504 1.00 8.64ATOM 937 O SER A 652 11.068 4.520 27.125 1.00 9.90 ATOM 938 N HIS A 6539.805 3.249 25.765 1.00 9.64 ATOM 939 CA HIS A 653 10.739 2.128 25.7691.00 9.99 ATOM 940 CB HIS A 653 10.164 0.963 24.952 1.00 8.26 ATOM 941CG HIS A 653 10.546 0.980 23.510 1.00 8.55 ATOM 942 CD2 HIS A 653 11.5290.333 22.842 1.00 9.53 ATOM 943 ND1 HIS A 653 9.881 1.740 22.569 1.0010.01 ATOM 944 CE1 HIS A 653 10.440 1.559 21.387 1.00 6.46 ATOM 945 NE2HIS A 653 11.444 0.708 21.526 1.00 6.65 ATOM 946 C HIS A 653 12.2102.321 25.412 1.00 10.62 ATOM 947 O HIS A 653 13.024 1.459 25.741 1.008.86 ATOM 948 N ASP A 654 12.559 3.424 24.752 1.00 9.82 ATOM 949 CA ASPA 654 13.959 3.673 24.406 1.00 9.46 ATOM 950 CB ASP A 654 14.184 3.58022.889 1.00 10.10 ATOM 951 CG ASP A 654 14.509 2.172 22.432 1.00 10.77ATOM 952 OD1 ASP A 654 15.159 1.444 23.204 1.00 9.55 ATOM 953 OD2 ASP A654 14.141 1.812 21.294 1.00 8.85 ATOM 954 C ASP A 654 14.477 5.02424.896 1.00 9.92 ATOM 955 O ASP A 654 15.500 5.507 24.413 1.00 9.67 ATOM956 N LEU A 655 13.783 5.619 25.865 1.00 9.19 ATOM 957 CA LEU A 65514.169 6.922 26.408 1.00 10.06 ATOM 958 CB LEU A 655 13.364 7.214 27.6771.00 8.55 ATOM 959 CG LEU A 655 11.900 7.603 27.479 1.00 10.24 ATOM 960CD1 LEU A 655 11.151 7.468 28.805 1.00 9.10 ATOM 961 CD2 LEU A 65511.819 9.028 26.944 1.00 15.71 ATOM 962 C LEU A 655 15.658 7.101 26.7131.00 10.50 ATOM 963 O LEU A 655 16.279 6.268 27.372 1.00 9.92 ATOM 964 NASP A 656 16.215 8.209 26.232 1.00 8.66 ATOM 965 CA ASP A 656 17.6228.542 26.448 1.00 8.66 ATOM 966 CB ASP A 656 17.867 8.811 27.941 1.0011.08 ATOM 967 CG ASP A 656 19.211 9.475 28.207 1.00 16.07 ATOM 968 OD1ASP A 656 19.576 10.406 27.460 1.00 11.04 ATOM 969 OD2 ASP A 656 19.8979.074 29.173 1.00 13.88 ATOM 970 C ASP A 656 18.600 7.483 25.939 1.008.59 ATOM 971 O ASP A 656 19.670 7.288 26.511 1.00 9.89 ATOM 972 N HIS A657 18.242 6.806 24.851 1.00 9.07 ATOM 973 CA HIS A 657 19.118 5.79024.284 1.00 10.63 ATOM 974 CB HIS A 657 18.412 5.068 23.137 1.00 9.06ATOM 975 CG HIS A 657 19.095 3.810 22.712 1.00 8.47 ATOM 976 CD2 HIS A657 20.347 3.589 22.245 1.00 7.97 ATOM 977 ND1 HIS A 657 18.480 2.57522.748 1.00 12.46 ATOM 978 CE1 HIS A 657 19.322 1.652 22.322 1.00 5.38ATOM 979 NE2 HIS A 657 20.464 2.242 22.011 1.00 12.33 ATOM 980 C HIS A657 20.404 6.453 23.778 1.00 11.40 ATOM 981 O HIS A 657 20.362 7.40422.993 1.00 11.45 ATOM 982 N PRO A 658 21.567 5.957 24.230 1.00 11.01ATOM 983 CD PRO A 658 21.697 4.963 25.311 1.00 10.94 ATOM 984 CA PRO A658 22.884 6.479 23.850 1.00 10.19 ATOM 985 CB PRO A 658 23.792 5.93024.944 1.00 9.66 ATOM 986 CG PRO A 658 23.171 4.618 25.252 1.00 16.61ATOM 987 C PRO A 658 23.386 6.123 22.451 1.00 11.02 ATOM 988 O PRO A 65824.428 6.627 22.021 1.00 12.41 ATOM 989 N GLY A 659 22.659 5.265 21.7441.00 8.82 ATOM 990 CA GLY A 659 23.080 4.888 20.405 1.00 8.78 ATOM 991 CGLY A 659 24.115 3.781 20.356 1.00 9.97 ATOM 992 O GLY A 659 24.7503.566 19.316 1.00 12.32 ATOM 993 N VAL A 660 24.305 3.095 21.480 1.008.93 ATOM 994 CA VAL A 660 25.248 1.983 21.564 1.00 9.69 ATOM 995 CB VALA 660 26.554 2.387 22.301 1.00 10.19 ATOM 996 CG1 VAL A 660 27.358 3.35521.434 1.00 12.07 ATOM 997 CG2 VAL A 660 26.236 3.020 23.642 1.00 12.93ATOM 998 C VAL A 660 24.545 0.834 22.289 1.00 10.76 ATOM 999 O VAL A 66023.601 1.059 23.052 1.00 10.23 ATOM 1000 N SER A 661 25.002 −0.39222.049 1.00 7.63 ATOM 1001 CA SER A 661 24.371 −1.577 22.624 1.00 10.33ATOM 1002 CB SER A 661 24.748 −2.801 21.793 1.00 8.76 ATOM 1003 OG SER A661 26.099 −3.151 22.021 1.00 9.56 ATOM 1004 C SER A 661 24.687 −1.86424.088 1.00 9.36 ATOM 1005 O SER A 661 25.549 −1.230 24.696 1.00 10.42ATOM 1006 N ASN A 662 23.969 −2.838 24.643 1.00 10.10 ATOM 1007 CA ASN A662 24.165 −3.261 26.026 1.00 8.94 ATOM 1008 CB ASN A 662 23.177 −4.36926.384 1.00 12.24 ATOM 1009 CG ASN A 662 21.832 −3.836 26.824 1.00 11.27ATOM 1010 OD1 ASN A 662 20.794 −4.457 26.592 1.00 19.20 ATOM 1011 ND2ASN A 662 21.844 −2.689 27.483 1.00 5.90 ATOM 1012 C ASN A 662 25.586−3.781 26.161 1.00 11.89 ATOM 1013 O ASN A 662 26.289 −3.459 27.116 1.0012.39 ATOM 1014 N GLN A 663 26.010 −4.598 25.199 1.00 10.34 ATOM 1015 CAGLN A 663 27.356 −5.139 25.246 1.00 11.06 ATOM 1016 CB GLN A 663 27.578−6.120 24.083 1.00 14.83 ATOM 1017 CG GLN A 663 26.677 −7.373 24.1971.00 25.28 ATOM 1018 CD GLN A 663 25.283 −7.191 23.575 1.00 24.96 ATOM1019 OE1 GLN A 663 24.919 −6.113 23.106 1.00 31.10 ATOM 1020 NE2 GLN A663 24.497 −8.271 23.572 1.00 46.85 ATOM 1021 C GLN A 663 28.422 −4.03925.236 1.00 13.51 ATOM 1022 O GLN A 663 29.439 −4.161 25.921 1.00 12.70ATOM 1023 N PHE A 664 28.184 −2.956 24.504 1.00 12.64 ATOM 1024 CA PHE A664 29.145 −1.852 24.465 1.00 11.20 ATOM 1025 CB PHE A 664 28.754 −0.83823.380 1.00 12.60 ATOM 1026 CG PHE A 664 29.669 0.355 23.296 1.00 15.21ATOM 1027 CD1 PHE A 664 29.554 1.407 24.198 1.00 13.93 ATOM 1028 CD2 PHEA 664 30.668 0.409 22.336 1.00 10.34 ATOM 1029 CE1 PHE A 664 30.4192.484 24.144 1.00 11.59 ATOM 1030 CE2 PHE A 664 31.541 1.487 22.275 1.0016.42 ATOM 1031 CZ PHE A 664 31.418 2.527 23.182 1.00 18.27 ATOM 1032 CPHE A 664 29.207 −1.171 25.830 1.00 11.75 ATOM 1033 O PHE A 664 30.290−0.818 26.306 1.00 11.28 ATOM 1034 N LEU A 665 28.046 −0.980 26.452 1.0011.17 ATOM 1035 CA LEU A 665 27.982 −0.346 27.768 1.00 11.46 ATOM 1036CB LEU A 665 26.524 −0.163 28.204 1.00 11.38 ATOM 1037 CG LEU A 66525.703 0.864 27.420 1.00 9.72 ATOM 1038 CD1 LEU A 665 24.304 0.95928.015 1.00 16.35 ATOM 1039 CD2 LEU A 665 26.399 2.215 27.470 1.00 13.26ATOM 1040 C LEU A 665 28.726 −1.200 28.793 1.00 13.75 ATOM 1041 O LEU A665 29.404 −0.686 29.681 1.00 11.85 ATOM 1042 N ILE A 666 28.591 −2.51228.661 1.00 12.41 ATOM 1043 CA ILE A 666 29.259 −3.444 29.559 1.00 13.52ATOM 1044 CB ILE A 666 28.773 −4.887 29.300 1.00 13.10 ATOM 1045 CG2 ILEA 666 29.667 −5.882 30.020 1.00 13.00 ATOM 1046 CG1 ILE A 666 27.322−5.036 29.761 1.00 10.73 ATOM 1047 CD1 ILE A 666 26.687 −6.346 29.3691.00 14.67 ATOM 1048 C ILE A 666 30.770 −3.381 29.356 1.00 11.71 ATOM1049 O ILE A 666 31.541 −3.297 30.317 1.00 14.40 ATOM 1050 N ASN A 66731.183 −3.408 28.094 1.00 12.52 ATOM 1051 CA ASN A 667 32.599 −3.38227.733 1.00 11.69 ATOM 1052 CB ASN A 667 32.745 −3.652 26.232 1.00 15.94ATOM 1053 CG ASN A 667 32.340 −5.065 25.848 1.00 13.91 ATOM 1054 OD1 ASNA 667 32.138 −5.363 24.669 1.00 17.63 ATOM 1055 ND2 ASN A 667 32.233−5.946 26.837 1.00 11.25 ATOM 1056 C ASN A 667 33.323 −2.090 28.091 1.0015.59 ATOM 1057 O ASN A 667 34.530 −2.104 28.355 1.00 16.72 ATOM 1058 NTHR A 668 32.601 −0.974 28.098 1.00 15.05 ATOM 1059 CA THR A 668 33.2110.308 28.428 1.00 16.29 ATOM 1060 CB THR A 668 32.670 1.432 27.520 1.0016.12 ATOM 1061 OG1 THR A 668 31.237 1.448 27.567 1.00 19.49 ATOM 1062CG2 THR A 668 33.133 1.207 26.078 1.00 15.93 ATOM 1063 C THR A 66832.995 0.672 29.895 1.00 18.10 ATOM 1064 O THR A 668 33.158 1.830 30.2971.00 20.65 ATOM 1065 N ASN A 669 32.617 −0.330 30.682 1.00 17.75 ATOM1066 CA ASN A 669 32.402 −0.177 32.115 1.00 20.15 ATOM 1067 CB ASN A 66933.749 0.053 32.797 1.00 28.92 ATOM 1068 CG ASN A 669 34.791 −0.95532.361 1.00 34.79 ATOM 1069 OD1 ASN A 669 34.619 −2.160 32.543 1.0040.75 ATOM 1070 ND2 ASN A 669 35.877 −0.468 31.772 1.00 36.76 ATOM 1071C ASN A 669 31.428 0.926 32.515 1.00 20.87 ATOM 1072 O ASN A 669 31.6901.696 33.443 1.00 21.59 ATOM 1073 N SER A 670 30.302 0.996 31.819 1.0017.34 ATOM 1074 CA SER A 670 29.286 1.992 32.120 1.00 19.60 ATOM 1075 CBSER A 670 28.103 1.836 31.160 1.00 18.96 ATOM 1076 OG SER A 670 27.0232.672 31.535 1.00 22.69 ATOM 1077 C SER A 670 28.803 1.787 33.551 1.0016.24 ATOM 1078 O SER A 670 28.755 0.655 34.041 1.00 14.46 ATOM 1079 NGLU A 671 28.455 2.879 34.227 1.00 18.45 ATOM 1080 CA GLU A 671 27.9512.775 35.589 1.00 19.69 ATOM 1081 CB GLU A 671 27.756 4.154 36.209 1.0017.48 ATOM 1082 CG GLU A 671 28.985 5.024 36.189 1.00 31.14 ATOM 1083 CDGLU A 671 28.901 6.156 37.191 1.00 32.78 ATOM 1084 OE1 GLU A 671 27.8306.796 37.291 1.00 31.62 ATOM 1085 OE2 GLU A 671 29.914 6.406 37.875 1.0026.52 ATOM 1086 C GLU A 671 26.611 2.058 35.549 1.00 18.77 ATOM 1087 OGLU A 671 26.253 1.332 36.482 1.00 19.75 ATOM 1088 N LEU A 672 25.8682.281 34.466 1.00 17.92 ATOM 1089 CA LEU A 672 24.569 1.646 34.279 1.0015.76 ATOM 1090 CB LEU A 672 23.954 2.067 32.942 1.00 12.50 ATOM 1091 CGLEU A 672 23.478 3.509 32.771 1.00 18.92 ATOM 1092 CD1 LEU A 672 23.1013.741 31.314 1.00 18.65 ATOM 1093 CD2 LEU A 672 22.292 3.766 33.678 1.0024.52 ATOM 1094 C LEU A 672 24.738 0.130 34.291 1.00 13.50 ATOM 1095 OLEU A 672 23.961 −0.586 34.912 1.00 12.92 ATOM 1096 N ALA A 673 25.755−0.358 33.590 1.00 13.11 ATOM 1097 CA ALA A 673 26.001 −1.792 33.5461.00 13.53 ATOM 1098 CB ALA A 673 27.169 −2.099 32.594 1.00 11.10 ATOM1099 C ALA A 673 26.318 −2.283 34.956 1.00 13.78 ATOM 1100 O ALA A 67325.925 −3.380 35.354 1.00 12.36 ATOM 1101 N LEU A 674 27.028 −1.45835.718 1.00 15.22 ATOM 1102 CA LEU A 674 27.394 −1.829 37.076 1.00 16.65ATOM 1103 CB LEU A 674 28.414 −0.832 37.632 1.00 18.96 ATOM 1104 CG LEUA 674 29.225 −1.323 38.832 1.00 26.52 ATOM 1105 CD1 LEU A 674 29.939−2.620 38.460 1.00 24.45 ATOM 1106 CD2 LEU A 674 30.231 −0.258 39.2461.00 20.57 ATOM 1107 C LEU A 674 26.152 −1.866 37.960 1.00 15.94 ATOM1108 O LEU A 674 25.930 −2.818 38.709 1.00 16.86 ATOM 1109 N MET A 67525.335 −0.822 37.851 1.00 19.35 ATOM 1110 CA MET A 675 24.107 −0.69438.627 1.00 18.57 ATOM 1111 CB MET A 675 23.413 0.641 38.312 1.00 29.02ATOM 1112 CG MET A 675 24.180 1.882 38.753 1.00 32.86 ATOM 1113 SD MET A675 23.766 3.373 37.785 1.00 38.23 ATOM 1114 CE MET A 675 22.129 3.76938.381 1.00 40.96 ATOM 1115 C MET A 675 23.133 −1.830 38.346 1.00 17.83ATOM 1116 O MET A 675 22.529 −2.383 39.265 1.00 17.84 ATOM 1117 N TYR A676 23.000 −2.184 37.073 1.00 15.75 ATOM 1118 CA TYR A 676 22.052 −3.21236.679 1.00 16.85 ATOM 1119 CB TYR A 676 21.293 −2.720 35.442 1.00 16.19ATOM 1120 CG TYR A 676 20.619 −1.374 35.668 1.00 20.30 ATOM 1121 CD1 TYRA 676 19.694 −1.197 36.691 1.00 31.51 ATOM 1122 CE1 TYR A 676 19.1070.045 36.922 1.00 18.89 ATOM 1123 CD2 TYR A 676 20.934 −0.276 34.8771.00 23.78 ATOM 1124 CE2 TYR A 676 20.354 0.962 35.097 1.00 27.90 ATOM1125 CZ TYR A 676 19.443 1.117 36.118 1.00 24.78 ATOM 1126 OH TYR A 67618.866 2.354 36.326 1.00 28.03 ATOM 1127 C TYR A 676 22.605 −4.62336.471 1.00 16.48 ATOM 1128 O TYR A 676 21.949 −5.478 35.872 1.00 15.88ATOM 1129 N ASN A 677 23.814 −4.863 36.968 1.00 16.14 ATOM 1130 CA ASN A677 24.433 −6.182 36.888 1.00 14.23 ATOM 1131 CB ASN A 677 23.666 −7.13837.812 1.00 21.33 ATOM 1132 CG ASN A 677 24.382 −8.452 38.022 1.00 29.37ATOM 1133 OD1 ASN A 677 25.570 −8.478 38.349 1.00 38.44 ATOM 1134 ND2ASN A 677 23.662 −9.555 37.847 1.00 42.62 ATOM 1135 C ASN A 677 24.516−6.765 35.474 1.00 15.05 ATOM 1136 O ASN A 677 24.332 −7.966 35.275 1.0014.59 ATOM 1137 N ASP A 678 24.802 −5.904 34.502 1.00 13.69 ATOM 1138 CAASP A 678 24.926 −6.302 33.100 1.00 16.08 ATOM 1139 CB ASP A 678 26.080−7.293 32.915 1.00 12.96 ATOM 1140 CG ASP A 678 27.430 −6.691 33.2341.00 18.27 ATOM 1141 OD1 ASP A 678 27.519 −5.452 33.377 1.00 16.21 ATOM1142 OD2 ASP A 678 28.406 −7.464 33.334 1.00 20.95 ATOM 1143 C ASP A 67823.667 −6.919 32.499 1.00 16.35 ATOM 1144 O ASP A 678 23.731 −7.50931.420 1.00 17.49 ATOM 1145 N GLU A 679 22.534 −6.790 33.184 1.00 14.03ATOM 1146 CA GLU A 679 21.278 −7.358 32.690 1.00 14.39 ATOM 1147 CB GLUA 679 20.567 −8.133 33.799 1.00 14.04 ATOM 1148 CG GLU A 679 21.314−9.351 34.300 1.00 22.79 ATOM 1149 CD GLU A 679 20.514 −10.128 35.3301.00 43.42 ATOM 1150 OE1 GLU A 679 19.464 −10.699 34.964 1.00 51.30 ATOM1151 OE2 GLU A 679 20.931 −10.162 36.507 1.00 41.34 ATOM 1152 C GLU A679 20.320 −6.301 32.151 1.00 12.89 ATOM 1153 O GLU A 679 19.873 −5.43032.895 1.00 13.61 ATOM 1154 N SER A 680 19.993 −6.401 30.863 1.00 10.87ATOM 1155 CA SER A 680 19.086 −5.456 30.209 1.00 12.50 ATOM 1156 CB SERA 680 17.627 −5.787 30.555 1.00 12.08 ATOM 1157 OG SER A 680 17.267−7.087 30.111 1.00 11.26 ATOM 1158 C SER A 680 19.409 −4.038 30.663 1.0011.78 ATOM 1159 O SER A 680 18.517 −3.280 31.045 1.00 12.76 ATOM 1160 NVAL A 681 20.693 −3.693 30.617 1.00 9.67 ATOM 1161 CA VAL A 681 21.183−2.386 31.049 1.00 7.19 ATOM 1162 CB VAL A 681 22.688 −2.248 30.725 1.0011.97 ATOM 1163 CG1 VAL A 681 23.219 −0.917 31.245 1.00 10.98 ATOM 1164CG2 VAL A 681 23.460 −3.423 31.346 1.00 12.93 ATOM 1165 C VAL A 68120.426 −1.195 30.453 1.00 9.58 ATOM 1166 O VAL A 681 19.870 −0.37831.185 1.00 10.02 ATOM 1167 N LEU A 681A 20.420 −1.094 29.128 1.00 9.51ATOM 1168 CA LEU A 681A 19.718 −0.011 28.443 1.00 10.16 ATOM 1169 CB LEUA 681A 19.773 −0.216 26.929 1.00 7.24 ATOM 1170 CG LEU A 681A 21.0790.035 26.178 1.00 9.74 ATOM 1171 CD1 LEU A 681A 20.979 −0.563 24.7881.00 13.02 ATOM 1172 CD2 LEU A 681A 21.345 1.526 26.102 1.00 15.84 ATOM1173 C LEU A 681A 18.253 0.049 28.851 1.00 8.34 ATOM 1174 O LEU A 681A17.725 1.118 29.174 1.00 10.62 ATOM 1175 N GLU A 682 17.599 −1.11028.834 1.00 10.08 ATOM 1176 CA GLU A 682 16.183 −1.191 29.161 1.00 7.57ATOM 1177 CB GLU A 682 15.667 −2.599 28.855 1.00 6.60 ATOM 1178 CG GLU A682 15.731 −2.954 27.348 1.00 8.78 ATOM 1179 CD GLU A 682 17.151 −3.19926.835 1.00 12.12 ATOM 1180 OE1 GLU A 682 18.001 −3.693 27.614 1.0010.38 ATOM 1181 OE2 GLU A 682 17.418 −2.919 25.646 1.00 10.27 ATOM 1182C GLU A 682 15.867 −0.773 30.594 1.00 8.81 ATOM 1183 O GLU A 682 14.829−0.158 30.854 1.00 7.94 ATOM 1184 N HIS A 683 16.752 −1.099 31.526 1.009.05 ATOM 1185 CA HIS A 683 16.531 −0.677 32.897 1.00 10.40 ATOM 1186 CBHIS A 683 17.561 −1.324 33.830 1.00 11.92 ATOM 1187 CG HIS A 683 17.161−2.686 34.296 1.00 10.38 ATOM 1188 CD2 HIS A 683 17.557 −3.920 33.9031.00 9.93 ATOM 1189 ND1 HIS A 683 16.172 −2.888 35.238 1.00 14.33 ATOM1190 CE1 HIS A 683 15.977 −4.183 35.400 1.00 7.54 ATOM 1191 NE2 HIS A683 16.806 −4.831 34.599 1.00 15.67 ATOM 1192 C HIS A 683 16.631 0.84632.925 1.00 11.08 ATOM 1193 O HIS A 683 15.868 1.512 33.621 1.00 10.48ATOM 1194 N HIS A 684 17.553 1.397 32.138 1.00 10.86 ATOM 1195 CA HIS A684 17.710 2.844 32.076 1.00 9.98 ATOM 1196 CB HIS A 684 18.941 3.23331.256 1.00 9.09 ATOM 1197 CG HIS A 684 19.229 4.697 31.284 1.00 8.54ATOM 1198 CD2 HIS A 684 19.399 5.555 32.322 1.00 5.20 ATOM 1199 ND1 HISA 684 19.313 5.467 30.142 1.00 17.15 ATOM 1200 CE1 HIS A 684 19.5186.728 30.474 1.00 9.30 ATOM 1201 NE2 HIS A 684 19.573 6.807 31.795 1.0015.79 ATOM 1202 C HIS A 684 16.473 3.502 31.465 1.00 9.44 ATOM 1203 OHIS A 684 16.020 4.542 31.941 1.00 11.75 ATOM 1204 N HIS A 685 15.9292.898 30.411 1.00 9.42 ATOM 1205 CA HIS A 685 14.740 3.447 29.757 1.007.57 ATOM 1206 CB HIS A 685 14.361 2.621 28.521 1.00 14.86 ATOM 1207 CGHIS A 685 15.472 2.468 27.521 1.00 7.24 ATOM 1208 CD2 HIS A 685 15.8461.402 26.773 1.00 9.32 ATOM 1209 ND1 HIS A 685 16.299 3.506 27.161 1.008.86 ATOM 1210 CE1 HIS A 685 17.141 3.088 26.227 1.00 14.03 ATOM 1211NE2 HIS A 685 16.886 1.819 25.974 1.00 8.62 ATOM 1212 C HIS A 685 13.5743.446 30.747 1.00 9.27 ATOM 1213 O HIS A 685 12.798 4.401 30.805 1.009.78 ATOM 1214 N PHE A 686 13.439 2.376 31.523 1.00 8.10 ATOM 1215 CAPHE A 686 12.351 2.314 32.507 1.00 10.05 ATOM 1216 CB PHE A 686 12.2910.923 33.151 1.00 8.82 ATOM 1217 CG PHE A 686 11.281 0.808 34.263 1.0010.55 ATOM 1218 CD1 PHE A 686 9.937 1.078 34.035 1.00 10.53 ATOM 1219CD2 PHE A 686 11.674 0.442 35.538 1.00 11.42 ATOM 1220 CE1 PHE A 6869.013 0.985 35.061 1.00 14.12 ATOM 1221 CE2 PHE A 686 10.754 0.34836.568 1.00 15.20 ATOM 1222 CZ PHE A 686 9.423 0.618 36.328 1.00 13.66ATOM 1223 C PHE A 686 12.554 3.391 33.570 1.00 9.59 ATOM 1224 O PHE A686 11.599 4.036 34.022 1.00 11.10 ATOM 1225 N ASP A 687 13.807 3.60333.965 1.00 10.38 ATOM 1226 CA ASP A 687 14.169 4.620 34.950 1.00 13.63ATOM 1227 CB ASP A 687 15.699 4.646 35.147 1.00 15.63 ATOM 1228 CG ASP A687 16.163 5.810 36.032 1.00 35.43 ATOM 1229 OD1 ASP A 687 15.842 5.81237.238 1.00 39.21 ATOM 1230 OD2 ASP A 687 16.855 6.721 35.514 1.00 46.67ATOM 1231 C ASP A 687 13.701 5.983 34.453 1.00 11.19 ATOM 1232 O ASP A687 13.079 6.742 35.191 1.00 12.63 ATOM 1233 N GLN A 688 14.026 6.26633.194 1.00 10.97 ATOM 1234 CA GLN A 688 13.664 7.531 32.571 1.00 10.87ATOM 1235 CB GLN A 688 14.331 7.623 31.193 1.00 15.23 ATOM 1236 CG GLN A688 15.844 7.876 31.260 1.00 11.96 ATOM 1237 CD GLN A 688 16.179 9.35031.456 1.00 14.39 ATOM 1238 OE1 GLN A 688 15.805 10.193 30.640 1.0020.66 ATOM 1239 NE2 GLN A 688 16.881 9.663 32.535 1.00 29.50 ATOM 1240 CGLN A 688 12.158 7.651 32.455 1.00 10.36 ATOM 1241 O GLN A 688 11.5878.729 32.641 1.00 10.53 ATOM 1242 N CYS A 689 11.495 6.536 32.160 1.008.48 ATOM 1243 CA CYS A 689 10.043 6.517 32.040 1.00 9.59 ATOM 1244 CBCYS A 689 9.558 5.097 31.706 1.00 11.54 ATOM 1245 SG CYS A 689 7.7724.940 31.573 1.00 11.98 ATOM 1246 C CYS A 689 9.406 7.005 33.343 1.0010.54 ATOM 1247 O CYS A 689 8.559 7.905 33.331 1.00 10.86 ATOM 1248 NLEU A 690 9.822 6.417 34.463 1.00 12.43 ATOM 1249 CA LEU A 690 9.3166.786 35.787 1.00 13.70 ATOM 1250 CB LEU A 690 9.968 5.912 36.863 1.0015.35 ATOM 1251 CG LEU A 690 9.620 4.423 36.853 1.00 18.35 ATOM 1252 CD1LEU A 690 10.326 3.723 38.008 1.00 25.25 ATOM 1253 CD2 LEU A 690 8.1184.248 36.969 1.00 17.06 ATOM 1254 C LEU A 690 9.605 8.247 36.093 1.0014.05 ATOM 1255 O LEU A 690 8.767 8.975 36.633 1.00 15.63 ATOM 1256 NMET A 691 10.817 8.681 35.750 1.00 13.87 ATOM 1257 CA MET A 691 11.25610.042 35.975 1.00 14.41 ATOM 1258 CB MET A 691 12.676 10.212 35.4111.00 14.62 ATOM 1259 CG MET A 691 13.371 11.496 35.757 1.00 32.36 ATOM1260 SD MET A 691 12.902 12.755 34.635 1.00 45.55 ATOM 1261 CE MET A 69113.918 12.471 33.200 1.00 37.72 ATOM 1262 C MET A 691 10.285 11.02435.336 1.00 13.72 ATOM 1263 O MET A 691 9.863 11.990 35.971 1.00 14.45ATOM 1264 N ILE A 692 9.903 10.758 34.091 1.00 10.48 ATOM 1265 CA ILE A692 8.980 11.644 33.400 1.00 9.98 ATOM 1266 CB ILE A 692 8.966 11.37131.895 1.00 10.00 ATOM 1267 CG2 ILE A 692 7.909 12.240 31.224 1.00 12.51ATOM 1268 CG1 ILE A 692 10.346 11.691 31.315 1.00 14.40 ATOM 1269 CD1ILE A 692 10.482 11.400 29.841 1.00 19.81 ATOM 1270 C ILE A 692 7.57811.534 33.973 1.00 10.09 ATOM 1271 O ILE A 692 6.906 12.547 34.166 1.0011.41 ATOM 1272 N LEU A 693 7.149 10.316 34.288 1.00 12.13 ATOM 1273 CALEU A 693 5.821 10.111 34.862 1.00 13.85 ATOM 1274 CB LEU A 693 5.5488.615 35.058 1.00 13.96 ATOM 1275 CG LEU A 693 5.212 7.826 33.789 1.0010.33 ATOM 1276 CD1 LEU A 693 5.183 6.335 34.082 1.00 17.28 ATOM 1277CD2 LEU A 693 3.868 8.305 33.243 1.00 9.40 ATOM 1278 C LEU A 693 5.64410.837 36.193 1.00 14.19 ATOM 1279 O LEU A 693 4.524 11.179 36.577 1.0016.64 ATOM 1280 N ASN A 694 6.747 11.073 36.893 1.00 16.46 ATOM 1281 CAASN A 694 6.697 11.755 38.183 1.00 16.63 ATOM 1282 CB ASN A 694 7.68611.116 39.159 1.00 20.12 ATOM 1283 CG ASN A 694 7.231 9.760 39.641 1.0024.99 ATOM 1284 OD1 ASN A 694 7.869 8.742 39.373 1.00 30.33 ATOM 1285ND2 ASN A 694 6.115 9.736 40.360 1.00 25.93 ATOM 1286 C ASN A 694 6.98913.247 38.101 1.00 18.31 ATOM 1287 O ASN A 694 6.855 13.958 39.093 1.0018.26 ATOM 1288 N SER A 695 7.395 13.721 36.930 1.00 16.05 ATOM 1289 CASER A 695 7.704 15.139 36.755 1.00 17.70 ATOM 1290 CB SER A 695 8.32115.376 35.376 1.00 19.30 ATOM 1291 OG SER A 695 9.607 14.793 35.298 1.0034.04 ATOM 1292 C SER A 695 6.471 16.022 36.914 1.00 15.83 ATOM 1293 OSER A 695 5.400 15.710 36.406 1.00 17.46 ATOM 1294 N PRO A 696 6.61117.144 37.630 1.00 18.97 ATOM 1295 CD PRO A 696 7.779 17.577 38.415 1.0026.97 ATOM 1296 CA PRO A 696 5.480 18.053 37.830 1.00 18.99 ATOM 1297 CBPRO A 696 6.113 19.220 38.579 1.00 22.14 ATOM 1298 CG PRO A 696 7.15418.534 39.414 1.00 28.71 ATOM 1299 C PRO A 696 4.866 18.480 36.498 1.0016.02 ATOM 1300 O PRO A 696 5.585 18.839 35.564 1.00 18.08 ATOM 1301 NGLY A 697 3.539 18.425 36.418 1.00 16.17 ATOM 1302 CA GLY A 697 2.84318.804 35.201 1.00 16.65 ATOM 1303 C GLY A 697 2.862 17.725 34.130 1.0014.72 ATOM 1304 O GLY A 697 2.283 17.901 33.060 1.00 15.86 ATOM 1305 NASN A 698 3.511 16.601 34.424 1.00 14.68 ATOM 1306 CA ASN A 698 3.62115.493 33.471 1.00 14.66 ATOM 1307 CB ASN A 698 5.099 15.209 33.174 1.0015.25 ATOM 1308 CG ASN A 698 5.760 16.304 32.365 1.00 19.94 ATOM 1309OD1 ASN A 698 5.883 16.199 31.146 1.00 13.89 ATOM 1310 ND2 ASN A 6986.186 17.367 33.039 1.00 16.33 ATOM 1311 C ASN A 698 2.990 14.198 33.9731.00 14.82 ATOM 1312 O ASN A 698 3.044 13.174 33.293 1.00 13.20 ATOM1313 N GLN A 699 2.379 14.243 35.151 1.00 13.46 ATOM 1314 CA GLN A 6991.807 13.041 35.749 1.00 14.53 ATOM 1315 CB GLN A 699 1.652 13.28137.251 1.00 16.25 ATOM 1316 CG GLN A 699 2.957 13.713 37.902 1.00 17.08ATOM 1317 CD GLN A 699 2.787 14.103 39.350 1.00 37.15 ATOM 1318 OE1 GLNA 699 2.147 15.105 39.661 1.00 41.13 ATOM 1319 NE2 GLN A 699 3.35713.307 40.248 1.00 41.91 ATOM 1320 C GLN A 699 0.499 12.522 35.158 1.0013.96 ATOM 1321 O GLN A 699 −0.567 12.676 35.754 1.00 15.67 ATOM 1322 NILE A 700 0.582 11.867 34.003 1.00 13.44 ATOM 1323 CA ILE A 700 −0.61711.348 33.356 1.00 14.25 ATOM 1324 CB ILE A 700 −0.345 10.974 31.8811.00 15.57 ATOM 1325 CG2 ILE A 700 0.010 12.222 31.086 1.00 15.78 ATOM1326 CG1 ILE A 700 0.777 9.941 31.793 1.00 16.74 ATOM 1327 CD1 ILE A 7000.940 9.361 30.407 1.00 12.98 ATOM 1328 C ILE A 700 −1.262 10.151 34.0641.00 13.88 ATOM 1329 O ILE A 700 −2.342 9.709 33.673 1.00 14.53 ATOM1330 N LEU A 701 −0.609 9.624 35.098 1.00 11.60 ATOM 1331 CA LEU A 701−1.169 8.495 35.845 1.00 14.58 ATOM 1332 CB LEU A 701 −0.150 7.35835.965 1.00 13.85 ATOM 1333 CG LEU A 701 0.310 6.673 34.677 1.00 11.07ATOM 1334 CD1 LEU A 701 1.270 5.539 35.031 1.00 13.34 ATOM 1335 CD2 LEUA 701 −0.895 6.128 33.921 1.00 12.89 ATOM 1336 C LEU A 701 −1.612 8.91437.247 1.00 13.75 ATOM 1337 O LEU A 701 −2.053 8.084 38.040 1.00 15.74ATOM 1338 N SER A 702 −1.497 10.201 37.547 1.00 15.74 ATOM 1339 CA SER A702 −1.872 10.717 38.860 1.00 18.36 ATOM 1340 CB SER A 702 −1.573 12.21738.949 1.00 20.19 ATOM 1341 OG SER A 702 −2.446 12.958 38.113 1.00 21.94ATOM 1342 C SER A 702 −3.347 10.490 39.176 1.00 19.34 ATOM 1343 O SER A702 −3.754 10.559 40.336 1.00 20.75 ATOM 1344 N GLY A 703 −4.144 10.22438.148 1.00 18.92 ATOM 1345 CA GLY A 703 −5.565 10.012 38.359 1.00 20.40ATOM 1346 C GLY A 703 −5.944 8.600 38.764 1.00 21.19 ATOM 1347 O GLY A703 −7.036 8.369 39.284 1.00 20.43 ATOM 1348 N LEU A 704 −5.045 7.64938.539 1.00 16.00 ATOM 1349 CA LEU A 704 −5.326 6.259 38.876 1.00 15.59ATOM 1350 CB LEU A 704 −4.262 5.335 38.278 1.00 9.29 ATOM 1351 CG LEU A704 −4.459 4.921 36.823 1.00 14.10 ATOM 1352 CD1 LEU A 704 −4.510 6.14335.926 1.00 17.73 ATOM 1353 CD2 LEU A 704 −3.312 3.998 36.418 1.00 11.19ATOM 1354 C LEU A 704 −5.419 5.993 40.368 1.00 16.40 ATOM 1355 O LEU A704 −4.773 6.659 41.178 1.00 16.88 ATOM 1356 N SER A 705 −6.233 5.00440.721 1.00 15.43 ATOM 1357 CA SER A 705 −6.395 4.621 42.111 1.00 15.96ATOM 1358 CB SER A 705 −7.556 3.640 42.268 1.00 15.57 ATOM 1359 OG SER A705 −7.242 2.402 41.658 1.00 15.44 ATOM 1360 C SER A 705 −5.092 3.94742.515 1.00 16.32 ATOM 1361 O SER A 705 −4.280 3.583 41.662 1.00 17.25ATOM 1362 N ILE A 706 −4.886 3.782 43.812 1.00 17.56 ATOM 1363 CA ILE A706 −3.666 3.164 44.292 1.00 16.88 ATOM 1364 CB ILE A 706 −3.679 3.08645.836 1.00 21.33 ATOM 1365 CG2 ILE A 706 −2.466 2.331 46.335 1.00 23.53ATOM 1366 CG1 ILE A 706 −3.712 4.507 46.411 1.00 21.96 ATOM 1367 CD1 ILEA 706 −3.892 4.577 47.918 1.00 22.24 ATOM 1368 C ILE A 706 −3.415 1.78243.685 1.00 16.48 ATOM 1369 O ILE A 706 −2.291 1.470 43.291 1.00 18.62ATOM 1370 N GLU A 707 −4.456 0.962 43.584 1.00 15.92 ATOM 1371 CA GLU A707 −4.304 −0.376 43.019 1.00 14.53 ATOM 1372 CB GLU A 707 −5.509 −1.25043.378 1.00 19.33 ATOM 1373 CG GLU A 707 −5.518 −1.682 44.836 1.00 24.82ATOM 1374 CD GLU A 707 −4.269 −2.460 45.214 1.00 31.26 ATOM 1375 OE1 GLUA 707 −4.029 −3.525 44.610 1.00 34.47 ATOM 1376 OE2 GLU A 707 −3.525−2.006 46.110 1.00 30.79 ATOM 1377 C GLU A 707 −4.093 −0.385 41.507 1.0014.27 ATOM 1378 O GLU A 707 −3.283 −1.156 41.002 1.00 15.02 ATOM 1379 NGLU A 708 −4.818 0.458 40.782 1.00 11.81 ATOM 1380 CA GLU A 708 −4.6440.495 39.337 1.00 12.49 ATOM 1381 CB GLU A 708 −5.756 1.317 38.673 1.0014.73 ATOM 1382 CG GLU A 708 −7.134 0.663 38.813 1.00 11.98 ATOM 1383 CDGLU A 708 −8.088 1.020 37.683 1.00 18.01 ATOM 1384 OE1 GLU A 708 −8.1212.196 37.274 1.00 19.76 ATOM 1385 OE2 GLU A 708 −8.816 0.120 37.216 1.0022.22 ATOM 1386 C GLU A 708 −3.264 1.054 38.996 1.00 14.00 ATOM 1387 OGLU A 708 −2.624 0.607 38.047 1.00 12.79 ATOM 1388 N TYR A 709 −2.7982.018 39.784 1.00 12.70 ATOM 1389 CA TYR A 709 −1.482 2.604 39.551 1.0013.42 ATOM 1390 CB TYR A 709 −1.204 3.724 40.557 1.00 12.05 ATOM 1391 CGTYR A 709 0.129 4.407 40.339 1.00 19.13 ATOM 1392 CD1 TYR A 709 0.3115.302 39.296 1.00 14.81 ATOM 1393 CE1 TYR A 709 1.530 5.928 39.091 1.0015.81 ATOM 1394 CD2 TYR A 709 1.207 4.149 41.174 1.00 17.39 ATOM 1395CE2 TYR A 709 2.427 4.767 40.978 1.00 18.97 ATOM 1396 CZ TYR A 709 2.5835.658 39.934 1.00 17.67 ATOM 1397 OH TYR A 709 3.793 6.284 39.737 1.0018.77 ATOM 1398 C TYR A 709 −0.424 1.515 39.708 1.00 15.44 ATOM 1399 OTYR A 709 0.452 1.348 38.855 1.00 15.06 ATOM 1400 N LYS A 710 −0.5200.774 40.808 1.00 15.25 ATOM 1401 CA LYS A 710 0.409 −0.311 41.095 1.0015.31 ATOM 1402 CB LYS A 710 −0.020 −1.026 42.379 1.00 22.10 ATOM 1403CG LYS A 710 0.809 −2.249 42.716 1.00 23.74 ATOM 1404 CD LYS A 710 0.299−2.931 43.978 1.00 33.24 ATOM 1405 CE LYS A 710 0.996 −4.263 44.204 1.0039.08 ATOM 1406 NZ LYS A 710 2.478 −4.117 44.248 1.00 42.37 ATOM 1407 CLYS A 710 0.474 −1.309 39.939 1.00 14.94 ATOM 1408 O LYS A 710 1.555−1.645 39.448 1.00 12.87 ATOM 1409 N THR A 711 −0.692 −1.777 39.506 1.0013.50 ATOM 1410 CA THR A 711 −0.783 −2.736 38.411 1.00 12.45 ATOM 1411CB THR A 711 −2.249 −3.092 38.128 1.00 17.44 ATOM 1412 OG1 THR A 711−2.791 −3.792 39.255 1.00 21.96 ATOM 1413 CG2 THR A 711 −2.365 −3.95336.872 1.00 16.75 ATOM 1414 C THR A 711 −0.161 −2.198 37.129 1.00 11.72ATOM 1415 O THR A 711 0.597 −2.896 36.442 1.00 13.19 ATOM 1416 N THR A712 −0.487 −0.954 36.809 1.00 11.15 ATOM 1417 CA THR A 712 0.015 −0.31935.599 1.00 13.99 ATOM 1418 CB THR A 712 −0.598 1.081 35.424 1.00 9.97ATOM 1419 OG1 THR A 712 −2.029 0.967 35.357 1.00 14.40 ATOM 1420 CG2 THRA 712 −0.088 1.729 34.133 1.00 12.92 ATOM 1421 C THR A 712 1.541 −0.22135.556 1.00 12.77 ATOM 1422 O THR A 712 2.158 −0.596 34.559 1.00 12.54ATOM 1423 N LEU A 713 2.156 0.275 36.625 1.00 12.50 ATOM 1424 CA LEU A713 3.612 0.384 36.638 1.00 11.02 ATOM 1425 CB LEU A 713 4.105 1.02337.940 1.00 13.58 ATOM 1426 CG LEU A 713 3.889 2.528 38.100 1.00 22.03ATOM 1427 CD1 LEU A 713 4.754 3.042 39.250 1.00 21.64 ATOM 1428 CD2 LEUA 713 4.261 3.241 36.809 1.00 27.88 ATOM 1429 C LEU A 713 4.298 −0.96736.438 1.00 13.04 ATOM 1430 O LEU A 713 5.340 −1.048 35.785 1.00 12.26ATOM 1431 N LYS A 714 3.718 −2.026 36.995 1.00 11.66 ATOM 1432 CA LYS A714 4.304 −3.356 36.852 1.00 12.24 ATOM 1433 CB LYS A 714 3.540 −4.38337.690 1.00 17.46 ATOM 1434 CG LYS A 714 3.582 −4.123 39.182 1.00 27.51ATOM 1435 CD LYS A 714 2.878 −5.236 39.939 1.00 33.99 ATOM 1436 CE LYS A714 2.899 −4.988 41.433 1.00 42.93 ATOM 1437 NZ LYS A 714 2.222 −6.09242.168 1.00 46.33 ATOM 1438 C LYS A 714 4.284 −3.784 35.390 1.00 12.70ATOM 1439 O LYS A 714 5.259 −4.338 34.886 1.00 12.91 ATOM 1440 N ILE A715 3.168 −3.525 34.717 1.00 10.95 ATOM 1441 CA ILE A 715 3.023 −3.86933.308 1.00 10.57 ATOM 1442 CB ILE A 715 1.586 −3.590 32.820 1.00 11.39ATOM 1443 CG2 ILE A 715 1.468 −3.896 31.339 1.00 11.35 ATOM 1444 CG1 ILEA 715 0.596 −4.450 33.613 1.00 12.69 ATOM 1445 CD1 ILE A 715 −0.854−4.130 33.332 1.00 13.44 ATOM 1446 C ILE A 715 4.017 −3.052 32.482 1.0010.34 ATOM 1447 O ILE A 715 4.676 −3.581 31.588 1.00 11.86 ATOM 1448 NILE A 716 4.133 −1.762 32.793 1.00 10.78 ATOM 1449 CA ILE A 716 5.069−0.886 32.081 1.00 9.90 ATOM 1450 CB ILE A 716 4.989 0.563 32.621 1.0010.08 ATOM 1451 CG2 ILE A 716 6.171 1.387 32.115 1.00 10.86 ATOM 1452CG1 ILE A 716 3.661 1.197 32.189 1.00 10.91 ATOM 1453 CD1 ILE A 7163.413 2.564 32.792 1.00 11.27 ATOM 1454 C ILE A 716 6.508 −1.393 32.1961.00 8.77 ATOM 1455 O ILE A 716 7.229 −1.487 31.199 1.00 9.34 ATOM 1456N LYS A 717 6.926 −1.724 33.413 1.00 9.18 ATOM 1457 CA LYS A 717 8.275−2.235 33.623 1.00 10.88 ATOM 1458 CB LYS A 717 8.489 −2.606 35.087 1.0012.47 ATOM 1459 CG LYS A 717 9.790 −3.366 35.337 1.00 14.78 ATOM 1460 CDLYS A 717 9.865 −3.864 36.775 1.00 17.70 ATOM 1461 CE LYS A 717 11.045−4.809 36.977 1.00 29.85 ATOM 1462 NZ LYS A 717 11.082 −5.374 38.3551.00 25.71 ATOM 1463 C LYS A 717 8.540 −3.469 32.752 1.00 10.54 ATOM1464 O LYS A 717 9.536 −3.524 32.041 1.00 10.05 ATOM 1465 N GLN A 7187.647 −4.451 32.847 1.00 11.40 ATOM 1466 CA GLN A 718 7.774 −5.68232.067 1.00 11.80 ATOM 1467 CB GLN A 718 6.635 −6.628 32.434 1.00 11.33ATOM 1468 CG GLN A 718 6.683 −6.965 33.899 1.00 14.75 ATOM 1469 CD GLN A718 7.954 −7.691 34.293 1.00 35.80 ATOM 1470 OE1 GLN A 718 8.774 −7.17635.053 1.00 49.66 ATOM 1471 NE2 GLN A 718 8.115 −8.909 33.784 1.00 43.62ATOM 1472 C GLN A 718 7.778 −5.422 30.559 1.00 9.82 ATOM 1473 O GLN A718 8.559 −6.027 29.831 1.00 9.86 ATOM 1474 N ALA A 719 6.920 −4.51830.108 1.00 8.83 ATOM 1475 CA ALA A 719 6.842 −4.205 28.686 1.00 10.49ATOM 1476 CB ALA A 719 5.657 −3.292 28.436 1.00 5.96 ATOM 1477 C ALA A719 8.129 −3.560 28.186 1.00 9.98 ATOM 1478 O ALA A 719 8.618 −3.89227.101 1.00 9.19 ATOM 1479 N ILE A 720 8.688 −2.641 28.971 1.00 7.25ATOM 1480 CA ILE A 720 9.920 −1.988 28.548 1.00 8.66 ATOM 1481 CB ILE A720 10.233 −0.753 29.426 1.00 10.86 ATOM 1482 CG2 ILE A 720 11.616−0.193 29.086 1.00 11.64 ATOM 1483 CG1 ILE A 720 9.164 0.320 29.181 1.0011.59 ATOM 1484 CD1 ILE A 720 9.367 1.605 29.976 1.00 12.21 ATOM 1485 CILE A 720 11.085 −2.974 28.580 1.00 10.02 ATOM 1486 O ILE A 720 11.883−3.040 27.641 1.00 8.95 ATOM 1487 N LEU A 721 11.178 −3.762 29.643 1.008.10 ATOM 1488 CA LEU A 721 12.264 −4.733 29.719 1.00 8.45 ATOM 1489 CBLEU A 721 12.251 −5.446 31.077 1.00 10.55 ATOM 1490 CG LEU A 721 12.613−4.553 32.267 1.00 13.26 ATOM 1491 CD1 LEU A 721 12.539 −5.350 33.5741.00 15.78 ATOM 1492 CD2 LEU A 721 14.006 −3.991 32.059 1.00 24.08 ATOM1493 C LEU A 721 12.173 −5.750 28.576 1.00 9.96 ATOM 1494 O LEU A 72113.195 −6.196 28.049 1.00 8.91 ATOM 1495 N ALA A 722 10.948 −6.08228.175 1.00 8.77 ATOM 1496 CA ALA A 722 10.715 −7.047 27.100 1.00 8.74ATOM 1497 CB ALA A 722 9.219 −7.218 26.879 1.00 9.06 ATOM 1498 C ALA A722 11.383 −6.648 25.786 1.00 10.10 ATOM 1499 O ALA A 722 11.704 −7.50724.965 1.00 13.26 ATOM 1500 N THR A 723 11.598 −5.350 25.585 1.00 8.97ATOM 1501 CA THR A 723 12.213 −4.884 24.344 1.00 10.94 ATOM 1502 CB THRA 723 11.943 −3.374 24.127 1.00 8.53 ATOM 1503 OG1 THR A 723 12.542−2.615 25.181 1.00 8.41 ATOM 1504 CG2 THR A 723 10.437 −3.114 24.1181.00 8.22 ATOM 1505 C THR A 723 13.713 −5.187 24.203 1.00 9.21 ATOM 1506O THR A 723 14.327 −4.862 23.186 1.00 12.03 ATOM 1507 N ASP A 724 14.308−5.797 25.223 1.00 9.75 ATOM 1508 CA ASP A 724 15.710 −6.203 25.133 1.007.82 ATOM 1509 CB ASP A 724 16.257 −6.533 26.525 1.00 12.18 ATOM 1510 CGASP A 724 17.648 −7.147 26.490 1.00 8.16 ATOM 1511 OD1 ASP A 724 18.232−7.299 25.394 1.00 11.70 ATOM 1512 OD2 ASP A 724 18.161 −7.481 27.5811.00 11.61 ATOM 1513 C ASP A 724 15.600 −7.475 24.293 1.00 8.26 ATOM1514 O ASP A 724 15.022 −8.459 24.742 1.00 10.28 ATOM 1515 N LEU A 72516.127 −7.452 23.073 1.00 9.50 ATOM 1516 CA LEU A 725 16.037 −8.61122.189 1.00 8.83 ATOM 1517 CB LEU A 725 16.791 −8.343 20.883 1.00 11.33ATOM 1518 CG LEU A 725 16.365 −9.236 19.717 1.00 16.17 ATOM 1519 CD1 LEUA 725 14.910 −8.953 19.367 1.00 12.02 ATOM 1520 CD2 LEU A 725 17.262−8.974 18.516 1.00 20.09 ATOM 1521 C LEU A 725 16.573 −9.880 22.849 1.0012.30 ATOM 1522 O LEU A 725 16.179 −10.994 22.498 1.00 11.52 ATOM 1523 NALA A 726 17.476 −9.712 23.806 1.00 11.08 ATOM 1524 CA ALA A 726 18.028−10.855 24.517 1.00 12.63 ATOM 1525 CB ALA A 726 19.104 −10.394 25.4891.00 21.41 ATOM 1526 C ALA A 726 16.918 −11.583 25.274 1.00 12.40 ATOM1527 O ALA A 726 16.914 −12.813 25.354 1.00 13.56 ATOM 1528 N LEU A 72715.985 −10.823 25.843 1.00 12.79 ATOM 1529 CA LEU A 727 14.884 −11.42126.591 1.00 14.99 ATOM 1530 CB LEU A 727 14.206 −10.380 27.485 1.0011.71 ATOM 1531 CG LEU A 727 15.096 −9.856 28.612 1.00 16.19 ATOM 1532CD1 LEU A 727 14.302 −8.925 29.511 1.00 13.74 ATOM 1533 CD2 LEU A 72715.631 −11.036 29.409 1.00 19.43 ATOM 1534 C LEU A 727 13.868 −12.04525.646 1.00 15.02 ATOM 1535 O LEU A 727 13.173 −12.996 26.005 1.00 15.57ATOM 1536 N TYR A 728 13.777 −11.500 24.438 1.00 12.38 ATOM 1537 CA TYRA 728 12.862 −12.038 23.435 1.00 12.71 ATOM 1538 CB TYR A 728 12.844−11.136 22.194 1.00 10.64 ATOM 1539 CG TYR A 728 12.303 −11.823 20.9601.00 12.57 ATOM 1540 CD1 TYR A 728 10.966 −12.197 20.875 1.00 14.71 ATOM1541 CE1 TYR A 728 10.473 −12.854 19.752 1.00 12.42 ATOM 1542 CD2 TYR A728 13.139 −12.124 19.888 1.00 13.44 ATOM 1543 CE2 TYR A 728 12.659−12.777 18.763 1.00 13.13 ATOM 1544 CZ TYR A 728 11.329 −13.142 18.6991.00 15.27 ATOM 1545 OH TYR A 728 10.857 −13.801 17.580 1.00 18.62 ATOM1546 C TYR A 728 13.350 −13.430 23.041 1.00 12.62 ATOM 1547 O TYR A 72812.588 −14.401 23.028 1.00 14.23 ATOM 1548 N ILE A 729 14.636 −13.52222.723 1.00 12.98 ATOM 1549 CA ILE A 729 15.232 −14.788 22.327 1.0013.19 ATOM 1550 CB ILE A 729 16.723 −14.595 21.983 1.00 14.56 ATOM 1551CG2 ILE A 729 17.395 −15.942 21.797 1.00 19.39 ATOM 1552 CG1 ILE A 72916.849 −13.727 20.727 1.00 18.02 ATOM 1553 CD1 ILE A 729 18.268 −13.30920.406 1.00 26.38 ATOM 1554 C ILE A 729 15.088 −15.826 23.439 1.00 15.70ATOM 1555 O ILE A 729 14.830 −17.001 23.178 1.00 14.36 ATOM 1556 N LYS A730 15.227 −15.375 24.681 1.00 15.21 ATOM 1557 CA LYS A 730 15.127−16.257 25.837 1.00 16.44 ATOM 1558 CB LYS A 730 15.657 −15.528 27.0751.00 21.43 ATOM 1559 CG LYS A 730 15.494 −16.291 28.376 1.00 27.38 ATOM1560 CD LYS A 730 16.133 −15.528 29.523 1.00 31.22 ATOM 1561 CE LYS A730 15.975 −16.267 30.839 1.00 36.43 ATOM 1562 NZ LYS A 730 16.672−15.556 31.947 1.00 41.27 ATOM 1563 C LYS A 730 13.727 −16.802 26.1331.00 16.48 ATOM 1564 O LYS A 730 13.573 −17.972 26.498 1.00 17.06 ATOM1565 N ARG A 731 12.707 −15.969 25.968 1.00 14.55 ATOM 1566 CA ARG A 73111.347 −16.395 26.283 1.00 15.57 ATOM 1567 CB ARG A 731 10.622 −15.29127.060 1.00 19.59 ATOM 1568 CG ARG A 731 11.309 −14.842 28.335 1.0018.25 ATOM 1569 CD ARG A 731 10.437 −13.846 29.086 1.00 33.93 ATOM 1570NE ARG A 731 9.209 −14.462 29.588 1.00 32.78 ATOM 1571 CZ ARG A 7318.168 −13.781 30.058 1.00 29.98 ATOM 1572 NH1 ARG A 731 8.197 −12.45630.091 1.00 30.21 ATOM 1573 NH2 ARG A 731 7.097 −14.426 30.501 1.0036.09 ATOM 1574 C ARG A 731 10.461 −16.807 25.118 1.00 12.75 ATOM 1575 OARG A 731 9.436 −17.454 25.325 1.00 15.30 ATOM 1576 N ARG A 732 10.841−16.445 23.897 1.00 13.21 ATOM 1577 CA ARG A 732 10.002 −16.759 22.7511.00 11.06 ATOM 1578 CB ARG A 732 10.589 −16.162 21.474 1.00 10.97 ATOM1579 CG ARG A 732 11.872 −16.812 21.021 1.00 12.09 ATOM 1580 CD ARG A732 12.325 −16.192 19.724 1.00 12.79 ATOM 1581 NE ARG A 732 13.525−16.822 19.193 1.00 13.80 ATOM 1582 CZ ARG A 732 13.919 −16.704 17.9301.00 20.20 ATOM 1583 NH1 ARG A 732 13.201 −15.980 17.077 1.00 23.11 ATOM1584 NH2 ARG A 732 15.025 −17.307 17.518 1.00 22.17 ATOM 1585 C ARG A732 9.751 −18.245 22.549 1.00 11.37 ATOM 1586 O ARG A 732 8.704 −18.62522.031 1.00 11.95 ATOM 1587 N GLY A 733 10.703 −19.078 22.962 1.00 13.25ATOM 1588 CA GLY A 733 10.543 −20.512 22.804 1.00 13.40 ATOM 1589 C GLYA 733 9.298 −21.009 23.508 1.00 14.10 ATOM 1590 O GLY A 733 8.543−21.823 22.970 1.00 15.18 ATOM 1591 N GLU A 734 9.080 −20.512 24.7191.00 11.89 ATOM 1592 CA GLU A 734 7.919 −20.900 25.505 1.00 14.43 ATOM1593 CB GLU A 734 7.988 −20.264 26.895 1.00 14.05 ATOM 1594 CG GLU A 7346.675 −20.312 27.661 1.00 18.08 ATOM 1595 CD GLU A 734 6.810 −19.82829.091 1.00 21.97 ATOM 1596 OE1 GLU A 734 7.742 −19.048 29.372 1.0019.31 ATOM 1597 OE2 GLU A 734 5.977 −20.221 29.932 1.00 32.96 ATOM 1598C GLU A 734 6.632 −20.478 24.806 1.00 14.65 ATOM 1599 O GLU A 734 5.663−21.235 24.760 1.00 14.67 ATOM 1600 N PHE A 735 6.631 −19.264 24.2671.00 15.01 ATOM 1601 CA PHE A 735 5.470 −18.729 23.566 1.00 11.90 ATOM1602 CB PHE A 735 5.743 −17.278 23.157 1.00 11.17 ATOM 1603 CG PHE A 7354.632 −16.635 22.366 1.00 16.06 ATOM 1604 CD1 PHE A 735 3.354 −16.51522.892 1.00 16.32 ATOM 1605 CD2 PHE A 735 4.885 −16.102 21.111 1.0013.68 ATOM 1606 CE1 PHE A 735 2.355 −15.869 22.178 1.00 13.80 ATOM 1607CE2 PHE A 735 3.897 −15.458 20.400 1.00 12.16 ATOM 1608 CZ PHE A 7352.631 −15.340 20.931 1.00 14.03 ATOM 1609 C PHE A 735 5.142 −19.56622.329 1.00 13.78 ATOM 1610 O PHE A 735 3.989 −19.946 22.117 1.00 13.01ATOM 1611 N PHE A 736 6.156 −19.853 21.517 1.00 12.56 ATOM 1612 CA PHE A736 5.952 −20.632 20.299 1.00 14.09 ATOM 1613 CB PHE A 736 7.242 −20.69119.472 1.00 15.66 ATOM 1614 CG PHE A 736 7.752 −19.342 19.031 1.00 17.77ATOM 1615 CD1 PHE A 736 6.888 −18.268 18.894 1.00 16.30 ATOM 1616 CD2PHE A 736 9.092 −19.166 18.701 1.00 14.18 ATOM 1617 CE1 PHE A 736 7.345−17.040 18.435 1.00 13.31 ATOM 1618 CE2 PHE A 736 9.558 −17.939 18.2421.00 13.12 ATOM 1619 CZ PHE A 736 8.686 −16.877 18.106 1.00 17.60 ATOM1620 C PHE A 736 5.483 −22.054 20.598 1.00 14.02 ATOM 1621 O PHE A 7364.653 −22.608 19.874 1.00 15.27 ATOM 1622 N GLU A 737 6.022 −22.64021.661 1.00 15.53 ATOM 1623 CA GLU A 737 5.667 −24.000 22.047 1.00 16.49ATOM 1624 CB GLU A 737 6.598 −24.493 23.155 1.00 18.16 ATOM 1625 CG GLUA 737 6.296 −25.908 23.623 1.00 32.20 ATOM 1626 CD GLU A 737 7.266−26.397 24.685 1.00 44.41 ATOM 1627 OE1 GLU A 737 7.368 −25.748 25.7481.00 43.95 ATOM 1628 OE2 GLU A 737 7.926 −27.433 24.457 1.00 45.00 ATOM1629 C GLU A 737 4.219 −24.105 22.505 1.00 16.86 ATOM 1630 O GLU A 7373.517 −25.050 22.137 1.00 18.64 ATOM 1631 N LEU A 738 3.774 −23.14423.308 1.00 15.93 ATOM 1632 CA LEU A 738 2.396 −23.140 23.791 1.00 14.96ATOM 1633 CB LEU A 738 2.137 −21.910 24.665 1.00 13.51 ATOM 1634 CG LEUA 738 2.817 −21.890 26.037 1.00 13.44 ATOM 1635 CD1 LEU A 738 2.813−20.474 26.589 1.00 14.08 ATOM 1636 CD2 LEU A 738 2.103 −22.844 26.9871.00 21.77 ATOM 1637 C LEU A 738 1.435 −23.137 22.610 1.00 15.65 ATOM1638 O LEU A 738 0.431 −23.854 22.610 1.00 17.64 ATOM 1639 N ILE A 7391.743 −22.323 21.604 1.00 13.75 ATOM 1640 CA ILE A 739 0.904 −22.23620.415 1.00 14.28 ATOM 1641 CB ILE A 739 1.388 −21.112 19.464 1.00 12.79ATOM 1642 CG2 ILE A 739 0.686 −21.224 18.118 1.00 23.84 ATOM 1643 CG1ILE A 739 1.122 −19.744 20.096 1.00 16.58 ATOM 1644 CD1 ILE A 739 1.656−18.576 19.279 1.00 13.81 ATOM 1645 C ILE A 739 0.925 −23.557 19.6541.00 16.17 ATOM 1646 O ILE A 739 −0.126 −24.107 19.309 1.00 18.24 ATOM1647 N ARG A 740 2.124 −24.075 19.410 1.00 15.35 ATOM 1648 CA ARG A 7402.274 −25.322 18.671 1.00 18.48 ATOM 1649 CB ARG A 740 3.758 −25.64818.474 1.00 23.15 ATOM 1650 CG ARG A 740 3.996 −26.804 17.508 1.00 35.46ATOM 1651 CD ARG A 740 5.475 −27.059 17.224 1.00 39.66 ATOM 1652 NE ARGA 740 6.174 −27.694 18.340 1.00 40.53 ATOM 1653 CZ ARG A 740 6.703−27.043 19.371 1.00 42.20 ATOM 1654 NH1 ARG A 740 6.623 −25.721 19.4411.00 52.88 ATOM 1655 NH2 ARG A 740 7.317 −27.718 20.335 1.00 44.19 ATOM1656 C ARG A 740 1.582 −26.495 19.360 1.00 19.41 ATOM 1657 O ARG A 7401.093 −27.410 18.698 1.00 18.06 ATOM 1658 N LYS A 741 1.539 −26.47020.686 1.00 18.03 ATOM 1659 CA LYS A 741 0.906 −27.553 21.430 1.00 18.11ATOM 1660 CB LYS A 741 1.696 −27.853 22.699 1.00 14.50 ATOM 1661 CG LYSA 741 3.074 −28.426 22.451 1.00 21.67 ATOM 1662 CD LYS A 741 3.717−28.812 23.763 1.00 23.36 ATOM 1663 CE LYS A 741 5.087 −29.430 23.5581.00 27.38 ATOM 1664 NZ LYS A 741 5.715 −29.747 24.871 1.00 23.91 ATOM1665 C LYS A 741 −0.540 −27.248 21.798 1.00 17.80 ATOM 1666 O LYS A 741−1.134 −27.940 22.623 1.00 18.63 ATOM 1667 N ASN A 742 −1.102 −26.21421.183 1.00 17.40 ATOM 1668 CA ASN A 742 −2.478 −25.822 21.456 1.0017.84 ATOM 1669 CB ASN A 742 −3.443 −26.841 20.849 1.00 16.88 ATOM 1670CG ASN A 742 −3.442 −26.801 19.335 1.00 15.02 ATOM 1671 OD1 ASN A 742−3.741 −25.772 18.733 1.00 28.97 ATOM 1672 ND2 ASN A 742 −3.100 −27.92318.709 1.00 20.44 ATOM 1673 C ASN A 742 −2.734 −25.671 22.949 1.00 17.96ATOM 1674 O ASN A 742 −3.727 −26.174 23.486 1.00 17.06 ATOM 1675 N GLN A743 −1.827 −24.964 23.615 1.00 16.68 ATOM 1676 CA GLN A 743 −1.937−24.727 25.045 1.00 17.92 ATOM 1677 CB GLN A 743 −0.738 −25.338 25.7771.00 20.38 ATOM 1678 CG GLN A 743 −0.461 −26.787 25.408 1.00 28.60 ATOM1679 CD GLN A 743 0.746 −27.350 26.131 1.00 30.94 ATOM 1680 OE1 GLN A743 1.775 −26.682 26.255 1.00 32.52 ATOM 1681 NE2 GLN A 743 0.634−28.588 26.602 1.00 20.21 ATOM 1682 C GLN A 743 −2.002 −23.233 25.3411.00 16.35 ATOM 1683 O GLN A 743 −2.175 −22.836 26.490 1.00 18.44 ATOM1684 N PHE A 744 −1.877 −22.407 24.307 1.00 16.26 ATOM 1685 CA PHE A 744−1.916 −20.959 24.501 1.00 19.79 ATOM 1686 CB PHE A 744 −1.627 −20.22923.184 1.00 21.58 ATOM 1687 CG PHE A 744 −1.465 −18.740 23.340 1.0017.97 ATOM 1688 CD1 PHE A 744 −0.441 −18.216 24.117 1.00 20.04 ATOM 1689CD2 PHE A 744 −2.345 −17.865 22.720 1.00 24.29 ATOM 1690 CE1 PHE A 744−0.298 −16.847 24.271 1.00 24.80 ATOM 1691 CE2 PHE A 744 −2.208 −16.49922.869 1.00 20.38 ATOM 1692 CZ PHE A 744 −1.184 −15.988 23.647 1.0026.24 ATOM 1693 C PHE A 744 −3.265 −20.515 25.060 1.00 19.74 ATOM 1694 OPHE A 744 −4.316 −20.860 24.526 1.00 21.03 ATOM 1695 N ASN A 745 −3.221−19.746 26.142 1.00 19.11 ATOM 1696 CA ASN A 745 −4.427 −19.260 26.7911.00 18.83 ATOM 1697 CB ASN A 745 −4.893 −20.270 27.839 1.00 14.11 ATOM1698 CG ASN A 745 −6.067 −19.764 28.653 1.00 17.45 ATOM 1699 OD1 ASN A745 −6.924 −19.042 28.143 1.00 22.19 ATOM 1700 ND2 ASN A 745 −6.120−20.152 29.921 1.00 30.84 ATOM 1701 C ASN A 745 −4.183 −17.906 27.4461.00 17.46 ATOM 1702 O ASN A 745 −3.518 −17.818 28.481 1.00 17.84 ATOM1703 N LEU A 746 −4.720 −16.857 26.826 1.00 16.56 ATOM 1704 CA LEU A 746−4.573 −15.497 27.323 1.00 18.48 ATOM 1705 CB LEU A 746 −5.163 −14.49526.323 1.00 15.11 ATOM 1706 CG LEU A 746 −4.319 −14.192 25.082 1.0017.98 ATOM 1707 CD1 LEU A 746 −5.031 −13.165 24.217 1.00 16.50 ATOM 1708CD2 LEU A 746 −2.960 −13.664 25.507 1.00 17.71 ATOM 1709 C LEU A 746−5.212 −15.284 28.688 1.00 21.08 ATOM 1710 O LEU A 746 −4.911 −14.30429.366 1.00 20.60 ATOM 1711 N GLU A 747 −6.098 −16.192 29.089 1.00 21.14ATOM 1712 CA GLU A 747 −6.748 −16.075 30.389 1.00 21.90 ATOM 1713 CB GLUA 747 −7.916 −17.058 30.504 1.00 20.33 ATOM 1714 CG GLU A 747 −9.179−16.586 29.813 1.00 31.82 ATOM 1715 CD GLU A 747 −10.324 −17.569 29.9591.00 40.12 ATOM 1716 OE1 GLU A 747 −10.550 −18.057 31.086 1.00 43.30ATOM 1717 OE2 GLU A 747 −11.003 −17.846 28.949 1.00 40.94 ATOM 1718 CGLU A 747 −5.740 −16.331 31.498 1.00 22.98 ATOM 1719 O GLU A 747 −5.885−15.826 32.612 1.00 23.46 ATOM 1720 N ASP A 748 −4.719 −17.124 31.1881.00 21.44 ATOM 1721 CA ASP A 748 −3.670 −17.424 32.151 1.00 21.15 ATOM1722 CB ASP A 748 −2.800 −18.579 31.651 1.00 19.25 ATOM 1723 CG ASP A748 −1.656 −18.899 32.595 1.00 19.90 ATOM 1724 OD1 ASP A 748 −0.710−18.088 32.692 1.00 26.86 ATOM 1725 OD2 ASP A 748 −1.704 −19.962 33.2461.00 42.46 ATOM 1726 C ASP A 748 −2.819 −16.171 32.314 1.00 20.94 ATOM1727 O ASP A 748 −2.240 −15.677 31.351 1.00 19.01 ATOM 1728 N PRO A 749−2.742 −15.637 33.541 1.00 18.53 ATOM 1729 CD PRO A 749 −3.443 −16.10834.750 1.00 26.08 ATOM 1730 CA PRO A 749 −1.958 −14.432 33.825 1.0019.83 ATOM 1731 CB PRO A 749 −2.009 −14.346 35.347 1.00 25.90 ATOM 1732CG PRO A 749 −3.377 −14.896 35.654 1.00 25.60 ATOM 1733 C PRO A 749−0.528 −14.476 33.286 1.00 17.96 ATOM 1734 O PRO A 749 −0.047 −13.50632.708 1.00 18.09 ATOM 1735 N HIS A 750 0.149 −15.603 33.475 1.00 17.27ATOM 1736 CA HIS A 750 1.520 −15.737 32.998 1.00 16.70 ATOM 1737 CB HISA 750 2.138 −17.039 33.509 1.00 14.57 ATOM 1738 CG HIS A 750 3.506−17.301 32.975 1.00 13.17 ATOM 1739 CD2 HIS A 750 4.710 −16.780 33.2991.00 15.22 ATOM 1740 ND1 HIS A 750 3.748 −18.181 31.933 1.00 20.55 ATOM1741 CE1 HIS A 750 5.030 −18.183 31.649 1.00 21.44 ATOM 1742 NE2 HIS A750 5.644 −17.338 32.465 1.00 27.33 ATOM 1743 C HIS A 750 1.615 −15.69131.475 1.00 16.04 ATOM 1744 O HIS A 750 2.521 −15.069 30.925 1.00 16.50ATOM 1745 N GLU A 751 0.680 −16.346 30.794 1.00 14.76 ATOM 1746 CA GLU A751 0.689 −16.359 29.333 1.00 14.97 ATOM 1747 CB GLU A 751 −0.269−17.427 28.798 1.00 11.89 ATOM 1748 CG GLU A 751 0.173 −18.848 29.1231.00 16.94 ATOM 1749 CD GLU A 751 −0.601 −19.892 28.354 1.00 17.06 ATOM1750 OE1 GLU A 751 −0.804 −19.697 27.140 1.00 17.15 ATOM 1751 OE2 GLU A751 −0.993 −20.912 28.959 1.00 27.83 ATOM 1752 C GLU A 751 0.325 −14.98828.764 1.00 14.11 ATOM 1753 O GLU A 751 0.782 −14.616 27.685 1.00 14.18ATOM 1754 N LYS A 752 −0.501 −14.248 29.498 1.00 13.06 ATOM 1755 CA LYSA 752 −0.900 −12.910 29.092 1.00 11.63 ATOM 1756 CB LYS A 752 −1.984−12.370 30.041 1.00 11.74 ATOM 1757 CG LYS A 752 −2.200 −10.865 29.9811.00 11.33 ATOM 1758 CD LYS A 752 −2.667 −10.402 28.608 1.00 18.51 ATOM1759 CE LYS A 752 −3.921 −11.138 28.184 1.00 31.49 ATOM 1760 NZ LYS A752 −4.536 −10.523 26.978 1.00 47.29 ATOM 1761 C LYS A 752 0.362 −12.04729.176 1.00 14.58 ATOM 1762 O LYS A 752 0.665 −11.293 28.249 1.00 11.11ATOM 1763 N GLU A 753 1.093 −12.196 30.270 1.00 12.46 ATOM 1764 CA GLU A753 2.315 −11.409 30.445 1.00 13.89 ATOM 1765 CB GLU A 753 2.939 −11.74531.801 1.00 15.41 ATOM 1766 CG GLU A 753 4.187 −10.950 32.098 1.00 17.51ATOM 1767 CD GLU A 753 4.946 −11.478 33.300 1.00 36.21 ATOM 1768 OE1 GLUA 753 4.335 −11.579 34.384 1.00 28.23 ATOM 1769 OE2 GLU A 753 6.150−11.782 33.162 1.00 36.81 ATOM 1770 C GLU A 753 3.267 −11.729 29.3131.00 14.45 ATOM 1771 O GLU A 753 3.852 −10.839 28.671 1.00 11.34 ATOM1772 N LEU A 754 3.441 −13.018 29.035 1.00 12.90 ATOM 1773 CA LEU A 7544.329 −13.471 27.974 1.00 13.51 ATOM 1774 CB LEU A 754 4.377 −15.01127.908 1.00 13.76 ATOM 1775 CG LEU A 754 5.196 −15.682 26.793 1.00 15.32ATOM 1776 CD1 LEU A 754 6.663 −15.286 26.877 1.00 15.56 ATOM 1777 CD2LEU A 754 5.044 −17.193 26.930 1.00 14.90 ATOM 1778 C LEU A 754 3.915−12.900 26.616 1.00 12.21 ATOM 1779 O LEU A 754 4.765 −12.478 25.8211.00 11.37 ATOM 1780 N PHE A 755 2.613 −12.867 26.351 1.00 11.00 ATOM1781 CA PHE A 755 2.119 −12.336 25.088 1.00 9.92 ATOM 1782 CB PHE A 7550.609 −12.551 24.966 1.00 12.44 ATOM 1783 CG PHE A 755 0.002 −11.86723.780 1.00 11.67 ATOM 1784 CD1 PHE A 755 0.338 −12.259 22.492 1.0013.36 ATOM 1785 CD2 PHE A 755 −0.858 −10.792 23.948 1.00 9.93 ATOM 1786CE1 PHE A 755 −0.170 −11.590 21.393 1.00 14.56 ATOM 1787 CE2 PHE A 755−1.369 −10.118 22.854 1.00 13.93 ATOM 1788 CZ PHE A 755 −1.021 −10.51721.574 1.00 18.65 ATOM 1789 C PHE A 755 2.431 −10.840 24.972 1.00 9.95ATOM 1790 O PHE A 755 2.856 −10.367 23.916 1.00 10.28 ATOM 1791 N LEU A756 2.225 −10.099 26.057 1.00 9.98 ATOM 1792 CA LEU A 756 2.489 −8.66426.034 1.00 9.03 ATOM 1793 CB LEU A 756 2.102 −8.017 27.370 1.00 9.14ATOM 1794 CG LEU A 756 0.610 −8.119 27.706 1.00 13.27 ATOM 1795 CD1 LEUA 756 0.331 −7.487 29.065 1.00 21.21 ATOM 1796 CD2 LEU A 756 −0.198−7.432 26.613 1.00 18.57 ATOM 1797 C LEU A 756 3.959 −8.410 25.721 1.009.36 ATOM 1798 O LEU A 756 4.291 −7.437 25.045 1.00 8.42 ATOM 1799 N ALAA 757 4.844 −9.285 26.197 1.00 7.41 ATOM 1800 CA ALA A 757 6.267 −9.11825.915 1.00 10.17 ATOM 1801 CB ALA A 757 7.096 −10.112 26.720 1.00 10.57ATOM 1802 C ALA A 757 6.514 −9.315 24.421 1.00 9.99 ATOM 1803 O ALA A757 7.254 −8.548 23.798 1.00 10.22 ATOM 1804 N MET A 758 5.890 −10.34123.845 1.00 8.41 ATOM 1805 CA MET A 758 6.046 −10.627 22.422 1.00 8.55ATOM 1806 CB MET A 758 5.348 −11.946 22.061 1.00 8.57 ATOM 1807 CG MET A758 5.898 −13.175 22.783 1.00 9.97 ATOM 1808 SD MET A 758 7.613 −13.59722.367 1.00 15.99 ATOM 1809 CE MET A 758 7.436 −14.226 20.702 1.00 36.66ATOM 1810 C MET A 758 5.469 −9.499 21.572 1.00 9.31 ATOM 1811 O MET A758 6.035 −9.134 20.534 1.00 8.67 ATOM 1812 N LEU A 759 4.334 −8.96222.008 1.00 10.68 ATOM 1813 CA LEU A 759 3.682 −7.877 21.290 1.00 7.26ATOM 1814 CB LEU A 759 2.348 −7.536 21.954 1.00 6.70 ATOM 1815 CG LEU A759 1.521 −6.419 21.316 1.00 9.88 ATOM 1816 CD1 LEU A 759 1.217 −6.75119.858 1.00 13.46 ATOM 1817 CD2 LEU A 759 0.232 −6.241 22.103 1.00 8.91ATOM 1818 C LEU A 759 4.589 −6.650 21.269 1.00 10.65 ATOM 1819 O LEU A759 4.677 −5.945 20.259 1.00 8.66 ATOM 1820 N MET A 760 5.258 −6.38822.387 1.00 8.87 ATOM 1821 CA MET A 760 6.168 −5.251 22.454 1.00 9.10ATOM 1822 CB MET A 760. 6.760 −5.114 23.859 1.00 9.37 ATOM 1823 CG MET A760 5.831 −4.491 24.889 1.00 7.94 ATOM 1824 SD MET A 760 5.392 −2.76224.513 1.00 11.15 ATOM 1825 CE MET A 760 6.981 −1.951 24.748 1.00 10.58ATOM 1826 C MET A 760 7.292 −5.445 21.444 1.00 9.36 ATOM 1827 O MET A760 7.693 −4.501 20.757 1.00 8.44 ATOM 1828 N THR A 761 7.812 −6.66721.359 1.00 8.62 ATOM 1829 CA THR A 761 8.890 −6.948 20.416 1.00 9.46ATOM 1830 CB THR A 761 9.442 −8.379 20.597 1.00 12.42 ATOM 1831 OG1 THRA 761 9.916 −8.540 21.940 1.00 11.86 ATOM 1832 CG2 THR A 761 10.598−8.636 19.620 1.00 9.90 ATOM 1833 C THR A 761 8.389 −6.785 18.984 1.0010.31 ATOM 1834 O THR A 761 9.088 −6.238 18.128 1.00 10.55 ATOM 1835 NALA A 762 7.172 −7.254 18.722 1.00 10.42 ATOM 1836 CA ALA A 762 6.598−7.148 17.389 1.00 7.73 ATOM 1837 CB ALA A 762 5.202 −7.777 17.362 1.0010.79 ATOM 1838 C ALA A 762 6.524 −5.689 16.948 1.00 9.57 ATOM 1839 OALA A 762 6.794 −5.370 15.787 1.00 9.59 ATOM 1840 N CYS A 763 6.161−4.801 17.872 1.00 7.53 ATOM 1841 CA CYS A 763 6.063 −3.378 17.551 1.007.89 ATOM 1842 CB CYS A 763 5.237 −2.641 18.611 1.00 11.70 ATOM 1843 SGCYS A 763 3.503 −3.143 18.670 1.00 11.19 ATOM 1844 C CYS A 763 7.441−2.744 17.443 1.00 9.03 ATOM 1845 O CYS A 763 7.689 −1.911 16.574 1.0010.26 ATOM 1846 N ASP A 764 8.340 −3.157 18.329 1.00 8.73 ATOM 1847 CAASP A 764 9.703 −2.641 18.352 1.00 10.03 ATOM 1848 CB ASP A 764 10.448−3.269 19.541 1.00 11.85 ATOM 1849 CG ASP A 764 11.766 −2.585 19.8401.00 12.03 ATOM 1850 OD1 ASP A 764 11.963 −1.451 19.361 1.00 11.46 ATOM1851 OD2 ASP A 764 12.592 −3.176 20.571 1.00 15.03 ATOM 1852 C ASP A 76410.447 −2.924 17.036 1.00 10.20 ATOM 1853 O ASP A 764 11.225 −2.09716.562 1.00 11.71 ATOM 1854 N LEU A 765 10.194 −4.086 16.442 1.00 11.54ATOM 1855 CA LEU A 765 10.867 −4.474 15.202 1.00 11.71 ATOM 1856 CB LEUA 765 11.208 −5.965 15.252 1.00 13.42 ATOM 1857 CG LEU A 765 12.017−6.454 16.453 1.00 15.02 ATOM 1858 CD1 LEU A 765 12.233 −7.957 16.3481.00 13.91 ATOM 1859 CD2 LEU A 765 13.345 −5.721 16.499 1.00 16.31 ATOM1860 C LEU A 765 10.049 −4.221 13.941 1.00 12.10 ATOM 1861 O LEU A 76510.490 −4.560 12.837 1.00 11.30 ATOM 1862 N SER A 766 8.881 −3.60614.101 1.00 12.76 ATOM 1863 CA SER A 766 7.965 −3.383 12.983 1.00 10.86ATOM 1864 CB SER A 766 6.672 −2.733 13.488 1.00 8.49 ATOM 1865 OG SER A766 6.902 −1.438 13.991 1.00 14.83 ATOM 1866 C SER A 766 8.446 −2.65711.729 1.00 7.60 ATOM 1867 O SER A 766 7.782 −2.735 10.700 1.00 9.56ATOM 1868 N ALA A 767 9.575 −1.956 11.787 1.00 8.02 ATOM 1869 CA ALA A767 10.073 −1.296 10.581 1.00 9.45 ATOM 1870 CB ALA A 767 11.364 −0.52210.881 1.00 11.41 ATOM 1871 C ALA A 767 10.340 −2.377 9.521 1.00 10.04ATOM 1872 O ALA A 767 10.253 −2.124 8.319 1.00 10.04 ATOM 1873 N ILE A768 10.655 −3.586 9.976 1.00 9.49 ATOM 1874 CA ILE A 768 10.942 −4.6949.066 1.00 12.99 ATOM 1875 CB ILE A 768 11.555 −5.894 9.840 1.00 9.64ATOM 1876 CG2 ILE A 768 10.473 −6.631 10.612 1.00 7.91 ATOM 1877 CG1 ILEA 768 12.270 −6.836 8.868 1.00 12.83 ATOM 1878 CD1 ILE A 768 13.471−6.199 8.190 1.00 15.69 ATOM 1879 C ILE A 768 9.704 −5.173 8.296 1.0011.57 ATOM 1880 O ILE A 768 9.812 −5.986 7.376 1.00 12.45 ATOM 1881 NTHR A 769 8.530 −4.665 8.662 1.00 12.70 ATOM 1882 CA THR A 769 7.286−5.062 7.999 1.00 10.88 ATOM 1883 CB THR A 769 6.167 −5.326 9.025 1.0013.25 ATOM 1884 OG1 THR A 769 5.760 −4.083 9.617 1.00 12.15 ATOM 1885CG2 THR A 769 6.654 −6.271 10.124 1.00 16.86 ATOM 1886 C THR A 769 6.762−3.991 7.036 1.00 12.18 ATOM 1887 O THR A 769 5.795 −4.223 6.308 1.0013.18 ATOM 1888 N LYS A 770 7.402 −2.824 7.043 1.00 12.64 ATOM 1889 CALYS A 770 6.986 −1.686 6.216 1.00 10.43 ATOM 1890 CB LYS A 770 7.684−0.413 6.714 1.00 12.22 ATOM 1891 CG LYS A 770 7.375 −0.029 8.165 1.007.87 ATOM 1892 CD LYS A 770 5.948 0.457 8.330 1.00 13.33 ATOM 1893 CELYS A 770 5.644 0.766 9.794 1.00 14.40 ATOM 1894 NZ LYS A 770 4.2631.293 9.973 1.00 14.45 ATOM 1895 C LYS A 770 7.247 −1.829 4.716 1.0011.91 ATOM 1896 O LYS A 770 8.069 −2.638 4.290 1.00 13.63 ATOM 1897 NPRO A 771 6.529 −1.041 3.892 1.00 11.52 ATOM 1898 CD PRO A 771 5.408−0.150 4.240 1.00 14.60 ATOM 1899 CA PRO A 771 6.718 −1.096 2.441 1.0012.80 ATOM 1900 CB PRO A 771 5.914 0.099 1.950 1.00 15.88 ATOM 1901 CGPRO A 771 4.751 0.098 2.886 1.00 11.15 ATOM 1902 C PRO A 771 8.206−0.933 2.183 1.00 14.66 ATOM 1903 O PRO A 771 8.880 −0.201 2.908 1.0015.01 ATOM 1904 N TRP A 772 8.711 −1.604 1.156 1.00 14.26 ATOM 1905 CATRP A 772 10.133 −1.555 0.827 1.00 15.34 ATOM 1906 CB TRP A 772 10.367−2.121 −0.578 1.00 14.10 ATOM 1907 CG TRP A 772 11.809 −2.101 −1.0091.00 17.47 ATOM 1908 CD2 TRP A 772 12.931 −2.659 −0.307 1.00 17.61 ATOM1909 CE2 TRP A 772 14.079 −2.404 −1.086 1.00 19.63 ATOM 1910 CE3 TRP A772 13.076 −3.348 0.901 1.00 16.69 ATOM 1911 CD1 TRP A 772 12.313 −1.547−2.152 1.00 16.69 ATOM 1912 NE1 TRP A 772 13.675 −1.725 −2.204 1.0024.41 ATOM 1913 CZ2 TRP A 772 15.354 −2.816 −0.694 1.00 24.29 ATOM 1914CZ3 TRP A 772 14.344 −3.755 1.289 1.00 17.48 ATOM 1915 CH2 TRP A 77215.466 −3.488 0.493 1.00 21.25 ATOM 1916 C TRP A 772 10.820 −0.190 0.9521.00 17.78 ATOM 1917 O TRP A 772 11.834 −0.070 1.639 1.00 15.81 ATOM1918 N PRO A 773 10.286 0.853 0.291 1.00 19.35 ATOM 1919 CD PRO A 7739.132 0.877 −0.624 1.00 18.85 ATOM 1920 CA PRO A 773 10.909 2.180 0.3771.00 18.24 ATOM 1921 CB PRO A 773 9.926 3.068 −0.382 1.00 21.17 ATOM1922 CG PRO A 773 9.386 2.138 −1.422 1.00 23.60 ATOM 1923 C PRO A 77311.129 2.654 1.814 1.00 16.33 ATOM 1924 O PRO A 773 12.167 3.235 2.1401.00 16.01 ATOM 1925 N ILE A 774 10.143 2.406 2.668 1.00 16.23 ATOM 1926CA ILE A 774 10.228 2.805 4.066 1.00 15.30 ATOM 1927 CB ILE A 774 8.8512.670 4.751 1.00 15.99 ATOM 1928 CG2 ILE A 774 8.977 2.922 6.250 1.0013.24 ATOM 1929 CG1 ILE A 774 7.867 3.658 4.110 1.00 20.68 ATOM 1930 CD1ILE A 774 6.441 3.501 4.588 1.00 21.74 ATOM 1931 C ILE A 774 11.2641.958 4.804 1.00 16.31 ATOM 1932 O ILE A 774 12.133 2.491 5.497 1.0015.63 ATOM 1933 N GLN A 775 11.173 0.640 4.650 1.00 13.80 ATOM 1934 CAGLN A 775 12.120 −0.274 5.279 1.00 12.85 ATOM 1935 CB GLN A 775 11.786−1.727 4.901 1.00 13.34 ATOM 1936 CG GLN A 775 12.987 −2.688 4.921 1.0014.20 ATOM 1937 CD GLN A 775 13.582 −2.897 6.305 1.00 21.70 ATOM 1938OE1 GLN A 775 14.663 −3.472 6.441 1.00 13.81 ATOM 1939 NE2 GLN A 77512.880 −2.440 7.336 1.00 14.50 ATOM 1940 C GLN A 775 13.549 0.057 4.8771.00 13.13 ATOM 1941 O GLN A 775 14.458 0.060 5.694 1.00 12.67 ATOM 1942N GLN A 776 13.749 0.352 3.590 1.00 10.04 ATOM 1943 CA GLN A 776 15.0680.674 3.090 1.00 12.84 ATOM 1944 CB GLN A 776 15.004 0.820 1.564 1.0019.00 ATOM 1945 CG GLN A 776 16.326 0.943 0.890 1.00 25.33 ATOM 1946 CDGLN A 776 16.172 0.760 −0.595 1.00 36.37 ATOM 1947 OE1 GLN A 776 15.2581.315 −1.209 1.00 39.80 ATOM 1948 NE2 GLN A 776 17.058 −0.023 −1.1861.00 41.16 ATOM 1949 C GLN A 776 15.627 1.934 3.738 1.00 10.61 ATOM 1950O GLN A 776 16.796 1.988 4.109 1.00 13.39 ATOM 1951 N ARG A 777 14.7762.946 3.922 1.00 10.52 ATOM 1952 CA ARG A 777 15.199 4.197 4.534 1.0011.43 ATOM 1953 CB ARG A 777 14.090 5.253 4.419 1.00 15.26 ATOM 1954 CGARG A 777 14.487 6.607 4.948 1.00 20.06 ATOM 1955 CD ARG A 777 13.3437.586 4.765 1.00 25.19 ATOM 1956 NE ARG A 777 12.206 7.273 5.627 1.0034.37 ATOM 1957 CZ ARG A 777 12.232 7.359 6.954 1.00 35.62 ATOM 1958 NH1ARG A 777 13.340 7.747 7.575 1.00 37.87 ATOM 1959 NH2 ARG A 777 11.1497.068 7.661 1.00 29.66 ATOM 1960 C ARG A 777 15.560 3.979 5.997 1.0010.83 ATOM 1961 O ARG A 777 16.601 4.447 6.472 1.00 13.15 ATOM 1962 NILE A 778 14.715 3.238 6.705 1.00 12.38 ATOM 1963 CA ILE A 778 14.9532.944 8.112 1.00 13.18 ATOM 1964 CB ILE A 778 13.753 2.209 8.744 1.0015.50 ATOM 1965 CG2 ILE A 778 14.091 1.788 10.170 1.00 13.56 ATOM 1966CG1 ILE A 778 12.516 3.108 8.721 1.00 22.29 ATOM 1967 CD1 ILE A 77812.685 4.399 9.478 1.00 26.81 ATOM 1968 C ILE A 778 16.198 2.086 8.3051.00 12.49 ATOM 1969 O ILE A 778 16.963 2.298 9.245 1.00 12.70 ATOM 1970N ALA A 779 16.399 1.117 7.417 1.00 12.47 ATOM 1971 CA ALA A 779 17.5630.242 7.510 1.00 13.19 ATOM 1972 CB ALA A 779 17.538 −0.789 6.391 1.0014.05 ATOM 1973 C ALA A 779 18.856 1.051 7.452 1.00 13.71 ATOM 1974 OALA A 779 19.839 0.700 8.106 1.00 11.99 ATOM 1975 N GLU A 780 18.8582.131 6.672 1.00 14.86 ATOM 1976 CA GLU A 780 20.048 2.976 6.560 1.0013.62 ATOM 1977 CB GLU A 780 19.860 4.053 5.487 1.00 17.29 ATOM 1978 CGGLU A 780 19.742 3.519 4.075 1.00 30.45 ATOM 1979 CD GLU A 780 19.7444.628 3.038 1.00 42.90 ATOM 1980 OE1 GLU A 780 20.761 5.347 2.939 1.0042.08 ATOM 1981 OE2 GLU A 780 18.728 4.783 2.326 1.00 56.88 ATOM 1982 CGLU A 780 20.350 3.649 7.897 1.00 13.45 ATOM 1983 O GLU A 780 21.5063.791 8.277 1.00 14.75 ATOM 1984 N LEU A 781 19.303 4.074 8.597 1.0012.82 ATOM 1985 CA LEU A 781 19.464 4.716 9.898 1.00 10.66 ATOM 1986 CBLEU A 781 18.113 5.215 10.410 1.00 12.60 ATOM 1987 CG LEU A 781 17.4286.296 9.574 1.00 15.49 ATOM 1988 CD1 LEU A 781 16.101 6.670 10.215 1.0014.52 ATOM 1989 CD2 LEU A 781 18.339 7.513 9.475 1.00 17.00 ATOM 1990 CLEU A 781 20.032 3.704 10.887 1.00 12.39 ATOM 1991 O LEU A 781 20.9354.014 11.673 1.00 11.98 ATOM 1992 N VAL A 782 19.490 2.490 10.839 1.009.90 ATOM 1993 CA VAL A 782 19.933 1.418 11.719 1.00 9.65 ATOM 1994 CBVAL A 782 19.116 0.126 11.463 1.00 10.42 ATOM 1995 CG1 VAL A 782 19.714−1.029 12.240 1.00 13.17 ATOM 1996 CG2 VAL A 782 17.657 0.339 11.8681.00 16.63 ATOM 1997 C VAL A 782 21.418 1.154 11.477 1.00 10.70 ATOM1998 O VAL A 782 22.210 1.068 12.418 1.00 13.37 ATOM 1999 N ALA A 78321.793 1.053 10.206 1.00 11.25 ATOM 2000 CA ALA A 783 23.185 0.810 9.8391.00 11.83 ATOM 2001 CB ALA A 783 23.299 0.632 8.337 1.00 15.10 ATOM2002 C ALA A 783 24.074 1.961 10.298 1.00 12.03 ATOM 2003 O ALA A 78325.170 1.746 10.820 1.00 12.81 ATOM 2004 N THR A 784 23.599 3.187 10.0991.00 11.94 ATOM 2005 CA THR A 784 24.358 4.359 10.504 1.00 10.90 ATOM2006 CB THR A 784 23.572 5.659 10.211 1.00 12.78 ATOM 2007 OG1 THR A 78423.359 5.778 8.797 1.00 15.62 ATOM 2008 CG2 THR A 784 24.341 6.88310.706 1.00 13.70 ATOM 2009 C THR A 784 24.676 4.282 11.995 1.00 11.74ATOM 2010 O THR A 784 25.819 4.490 12.408 1.00 10.51 ATOM 2011 N GLU A785 23.670 3.969 12.805 1.00 10.01 ATOM 2012 CA GLU A 785 23.881 3.88014.243 1.00 10.75 ATOM 2013 CB GLU A 785 22.549 3.669 14.968 1.00 7.51ATOM 2014 CG GLU A 785 22.675 3.740 16.483 1.00 9.65 ATOM 2015 CD GLU A785 21.335 3.755 17.178 1.00 7.52 ATOM 2016 OE1 GLU A 785 20.415 4.43616.674 1.00 10.93 ATOM 2017 OE2 GLU A 785 21.208 3.099 18.236 1.00 12.56ATOM 2018 C GLU A 785 24.847 2.760 14.612 1.00 11.99 ATOM 2019 O GLU A785 25.737 2.948 15.440 1.00 11.68 ATOM 2020 N PHE A 786 24.671 1.59413.997 1.00 9.83 ATOM 2021 CA PHE A 786 25.541 0.464 14.285 1.00 10.39ATOM 2022 CB PHE A 786 25.069 −0.794 13.550 1.00 11.58 ATOM 2023 CG PHEA 786 23.876 −1.455 14.176 1.00 16.59 ATOM 2024 CD1 PHE A 786 23.632−1.327 15.533 1.00 18.18 ATOM 2025 CD2 PHE A 786 23.034 −2.254 13.4191.00 19.90 ATOM 2026 CE1 PHE A 786 22.570 −1.986 16.125 1.00 25.35 ATOM2027 CE2 PHE A 786 21.972 −2.916 14.004 1.00 17.12 ATOM 2028 CZ PHE A786 21.740 −2.781 15.360 1.00 16.84 ATOM 2029 C PHE A 786 26.985 0.76013.898 1.00 9.62 ATOM 2030 O PHE A 786 27.907 0.444 14.652 1.00 10.46ATOM 2031 N PHE A 787 27.183 1.348 12.720 1.00 8.90 ATOM 2032 CA PHE A787 28.531 1.680 12.273 1.00 9.83 ATOM 2033 CB PHE A 787 28.515 2.14110.809 1.00 10.96 ATOM 2034 CG PHE A 787 28.116 1.056 9.849 1.00 8.28ATOM 2035 CD1 PHE A 787 28.335 −0.276 10.172 1.00 10.72 ATOM 2036 CD2PHE A 787 27.546 1.357 8.626 1.00 11.47 ATOM 2037 CE1 PHE A 787 27.993−1.287 9.296 1.00 12.45 ATOM 2038 CE2 PHE A 787 27.201 0.344 7.739 1.0012.21 ATOM 2039 CZ PHE A 787 27.424 −0.977 8.075 1.00 8.97 ATOM 2040 CPHE A 787 29.165 2.747 13.149 1.00 12.00 ATOM 2041 O PHE A 787 30.3872.787 13.311 1.00 11.70 ATOM 2042 N ASP A 788 28.340 3.620 13.713 1.0010.51 ATOM 2043 CA ASP A 788 28.867 4.655 14.583 1.00 13.07 ATOM 2044 CBASP A 788 27.770 5.654 14.953 1.00 9.28 ATOM 2045 CG ASP A 788 28.2756.751 15.869 1.00 17.65 ATOM 2046 OD1 ASP A 788 27.862 6.784 17.046 1.0022.26 ATOM 2047 OD2 ASP A 788 29.097 7.575 15.414 1.00 23.70 ATOM 2048 CASP A 788 29.427 3.975 15.832 1.00 11.61 ATOM 2049 O ASP A 788 30.4914.349 16.324 1.00 11.23 ATOM 2050 N GLN A 789 28.719 2.965 16.338 1.0010.39 ATOM 2051 CA GLN A 789 29.201 2.243 17.515 1.00 10.66 ATOM 2052 CBGLN A 789 28.185 1.199 17.979 1.00 14.04 ATOM 2053 CG GLN A 789 28.6670.416 19.191 1.00 13.95 ATOM 2054 CD GLN A 789 27.696 −0.652 19.641 1.0013.88 ATOM 2055 OE1 GLN A 789 26.488 −0.445 19.641 1.00 10.68 ATOM 2056NE2 GLN A 789 28.226 −1.799 20.051 1.00 10.88 ATOM 2057 C GLN A 78930.509 1.541 17.155 1.00 12.25 ATOM 2058 O GLN A 789 31.452 1.504 17.9521.00 12.92 ATOM 2059 N GLY A 790 30.552 0.979 15.950 1.00 12.27 ATOM2060 CA GLY A 790 31.746 0.292 15.493 1.00 13.69 ATOM 2061 C GLY A 79032.948 1.218 15.519 1.00 12.41 ATOM 2062 O GLY A 790 34.050 0.805 15.8851.00 14.19 ATOM 2063 N ASP A 791 32.743 2.476 15.135 1.00 13.24 ATOM2064 CA ASP A 791 33.837 3.448 15.135 1.00 15.89 ATOM 2065 CB ASP A 79133.383 4.802 14.582 1.00 11.78 ATOM 2066 CG ASP A 791 33.022 4.74813.108 1.00 11.72 ATOM 2067 OD1 ASP A 791 33.525 3.853 12.401 1.00 16.07ATOM 2068 OD2 ASP A 791 32.249 5.619 12.657 1.00 16.56 ATOM 2069 C ASP A791 34.350 3.653 16.554 1.00 15.06 ATOM 2070 O ASP A 791 35.555 3.75116.794 1.00 15.97 ATOM 2071 N ARG A 792 33.423 3.723 17.496 1.00 16.00ATOM 2072 CA ARG A 792 33.783 3.925 18.885 1.00 13.38 ATOM 2073 CB ARG A792 32.544 4.308 19.680 1.00 15.67 ATOM 2074 CG ARG A 792 32.056 5.68919.304 1.00 20.98 ATOM 2075 CD ARG A 792 30.791 6.043 20.014 1.00 22.55ATOM 2076 NE ARG A 792 30.929 6.004 21.465 1.00 21.96 ATOM 2077 CZ ARG A792 29.945 6.332 22.290 1.00 19.00 ATOM 2078 NH1 ARG A 792 28.782 6.72621.791 1.00 18.95 ATOM 2079 NH2 ARG A 792 30.105 6.236 23.601 1.00 23.88ATOM 2080 C ARG A 792 34.466 2.716 19.501 1.00 13.13 ATOM 2081 O ARG A792 35.296 2.865 20.390 1.00 14.33 ATOM 2082 N GLU A 793 34.112 1.52219.036 1.00 14.11 ATOM 2083 CA GLU A 793 34.730 0.305 19.545 1.00 12.55ATOM 2084 CB GLU A 793 33.969 −0.932 19.051 1.00 12.93 ATOM 2085 CG GLUA 793 32.531 −0.986 19.543 1.00 15.09 ATOM 2086 CD GLU A 793 31.816−2.269 19.165 1.00 17.10 ATOM 2087 OE1 GLU A 793 32.105 −2.807 18.0781.00 14.75 ATOM 2088 OE2 GLU A 793 30.951 −2.728 19.949 1.00 13.37 ATOM2089 C GLU A 793 36.184 0.251 19.080 1.00 13.70 ATOM 2090 O GLU A 79337.073 −0.143 19.837 1.00 14.48 ATOM 2091 N ARG A 794 36.429 0.65517.838 1.00 12.88 ATOM 2092 CA ARG A 794 37.792 0.647 17.318 1.00 16.50ATOM 2093 CB ARG A 794 37.828 1.083 15.847 1.00 16.91 ATOM 2094 CG ARG A794 37.330 0.047 14.838 1.00 16.40 ATOM 2095 CD ARG A 794 37.399 0.60913.422 1.00 20.95 ATOM 2096 NE ARG A 794 36.790 −0.268 12.422 1.00 21.25ATOM 2097 CZ ARG A 794 37.323 −1.407 11.996 1.00 16.41 ATOM 2098 NH1 ARGA 794 38.486 −1.822 12.480 1.00 26.91 ATOM 2099 NH2 ARG A 794 36.691−2.134 11.082 1.00 18.30 ATOM 2100 C ARG A 794 38.648 1.603 18.141 1.0017.48 ATOM 2101 O ARG A 794 39.781 1.287 18.503 1.00 18.61 ATOM 2102 NLYS A 795 38.087 2.769 18.443 1.00 19.00 ATOM 2103 CA LYS A 795 38.7933.795 19.199 1.00 19.03 ATOM 2104 CB LYS A 795 38.146 5.161 18.947 1.0022.77 ATOM 2105 CG LYS A 795 38.839 6.312 19.661 1.00 30.54 ATOM 2106 CDLYS A 795 38.128 7.633 19.410 1.00 38.45 ATOM 2107 CE LYS A 795 38.9028.796 20.009 1.00 34.57 ATOM 2108 NZ LYS A 795 40.267 8.886 19.424 1.0042.21 ATOM 2109 C LYS A 795 38.866 3.554 20.704 1.00 19.86 ATOM 2110 OLYS A 795 39.923 3.716 21.310 1.00 21.68 ATOM 2111 N GLU A 796 37.7473.166 21.304 1.00 17.50 ATOM 2112 CA GLU A 796 37.696 2.953 22.745 1.0018.20 ATOM 2113 CB GLU A 796 36.286 3.272 23.255 1.00 16.63 ATOM 2114 CGGLU A 796 35.872 4.722 23.048 1.00 19.55 ATOM 2115 CD GLU A 796 34.4254.982 23.414 1.00 17.22 ATOM 2116 OE1 GLU A 796 33.986 4.520 24.489 1.0017.11 ATOM 2117 OE2 GLU A 796 33.729 5.660 22.629 1.00 17.31 ATOM 2118 CGLU A 796 38.116 1.568 23.238 1.00 18.82 ATOM 2119 O GLU A 796 38.6041.432 24.359 1.00 19.88 ATOM 2120 N LEU A 797 37.936 0.544 22.408 1.0017.76 ATOM 2121 CA LEU A 797 38.279 −0.817 22.809 1.00 17.55 ATOM 2122CB LEU A 797 37.032 −1.708 22.732 1.00 14.21 ATOM 2123 CG LEU A 79735.816 −1.230 23.535 1.00 21.04 ATOM 2124 CD1 LEU A 797 34.655 −2.19423.333 1.00 19.81 ATOM 2125 CD2 LEU A 797 36.177 −1.134 25.008 1.0022.47 ATOM 2126 C LEU A 797 39.400 −1.441 21.980 1.00 18.06 ATOM 2127 OLEU A 797 39.899 −2.518 22.312 1.00 18.10 ATOM 2128 N ASN A 798 39.795−0.760 20.910 1.00 17.87 ATOM 2129 CA ASN A 798 40.846 −1.244 20.0161.00 17.14 ATOM 2130 CB ASN A 798 42.202 −1.278 20.732 1.00 18.53 ATOM2131 CG ASN A 798 43.357 −1.501 19.770 1.00 19.84 ATOM 2132 OD1 ASN A798 43.497 −0.774 18.788 1.00 22.65 ATOM 2133 ND2 ASN A 798 44.186−2.507 20.043 1.00 17.46 ATOM 2134 C ASN A 798 40.522 −2.632 19.472 1.0019.40 ATOM 2135 O ASN A 798 41.400 −3.485 19.352 1.00 18.37 ATOM 2136 NILE A 799 39.254 −2.852 19.141 1.00 18.23 ATOM 2137 CA ILE A 799 38.816−4.134 18.603 1.00 20.72 ATOM 2138 CB ILE A 799 37.779 −4.811 19.5291.00 23.69 ATOM 2139 CG2 ILE A 799 38.348 −4.970 20.930 1.00 25.12 ATOM2140 CG1 ILE A 799 36.500 −3.968 19.570 1.00 27.29 ATOM 2141 CD1 ILE A799 35.381 −4.581 20.373 1.00 23.09 ATOM 2142 C ILE A 799 38.158 −3.92617.243 1.00 20.66 ATOM 2143 O ILE A 799 37.636 −2.846 16.956 1.00 20.48ATOM 2144 N GLU A 800 38.199 −4.951 16.399 1.00 20.84 ATOM 2145 CA GLU A800 37.558 −4.855 15.096 1.00 19.43 ATOM 2146 CB GLU A 800 38.162 −5.85614.109 1.00 25.89 ATOM 2147 CG GLU A 800 37.507 −5.813 12.735 1.00 37.89ATOM 2148 CD GLU A 800 38.245 −6.637 11.699 1.00 48.08 ATOM 2149 OE1 GLUA 800 38.421 −7.856 11.915 1.00 47.23 ATOM 2150 OE2 GLU A 800 38.647−6.063 10.663 1.00 52.27 ATOM 2151 C GLU A 800 36.095 −5.188 15.345 1.0016.86 ATOM 2152 O GLU A 800 35.774 −6.249 15.879 1.00 20.00 ATOM 2153 NPRO A 801 35.186 −4.277 14.979 1.00 16.72 ATOM 2154 CD PRO A 801 35.413−2.971 14.340 1.00 13.94 ATOM 2155 CA PRO A 801 33.755 −4.518 15.1881.00 15.17 ATOM 2156 CB PRO A 801 33.101 −3.242 14.651 1.00 11.35 ATOM2157 CG PRO A 801 34.189 −2.204 14.760 1.00 18.39 ATOM 2158 C PRO A 80133.249 −5.750 14.446 1.00 14.88 ATOM 2159 O PRO A 801 33.836 −6.16813.437 1.00 14.57 ATOM 2160 N THR A 802 32.166 −6.333 14.952 1.00 13.89ATOM 2161 CA THR A 802 31.554 −7.473 14.282 1.00 13.70 ATOM 2162 CB THRA 802 30.367 −8.057 15.090 1.00 18.66 ATOM 2163 OG1 THR A 802 29.339−7.067 15.227 1.00 22.82 ATOM 2164 CG2 THR A 802 30.824 −8.491 16.4751.00 28.52 ATOM 2165 C THR A 802 31.028 −6.886 12.974 1.00 13.06 ATOM2166 O THR A 802 30.896 −5.666 12.853 1.00 13.12 ATOM 2167 N ASP A 80330.730 −7.737 11.997 1.00 13.68 ATOM 2168 CA ASP A 803 30.239 −7.26010.706 1.00 13.10 ATOM 2169 CB ASP A 803 29.784 −8.436 9.840 1.00 15.94ATOM 2170 CG ASP A 803 30.942 −9.281 9.340 1.00 19.70 ATOM 2171 OD1 ASPA 803 32.108 −8.965 9.661 1.00 16.86 ATOM 2172 OD2 ASP A 803 30.681−10.265 8.619 1.00 17.57 ATOM 2173 C ASP A 803 29.092 −6.262 10.829 1.0014.26 ATOM 2174 O ASP A 803 29.071 −5.239 10.141 1.00 15.59 ATOM 2175 NLEU A 804 28.142 −6.561 11.706 1.00 12.76 ATOM 2176 CA LEU A 804 26.982−5.700 11.907 1.00 13.21 ATOM 2177 CB LEU A 804 26.116 −6.251 13.0421.00 14.65 ATOM 2178 CG LEU A 804 24.861 −5.430 13.347 1.00 15.24 ATOM2179 CD1 LEU A 804 24.020 −5.317 12.092 1.00 16.29 ATOM 2180 CD2 LEU A804 24.068 −6.089 14.461 1.00 23.77 ATOM 2181 C LEU A 804 27.356 −4.25212.214 1.00 13.48 ATOM 2182 O LEU A 804 26.646 −3.317 11.825 1.00 13.22ATOM 2183 N MET A 805 28.476 −4.067 12.904 1.00 12.28 ATOM 2184 CA MET A805 28.909 −2.725 13.276 1.00 11.75 ATOM 2185 CB MET A 805 29.141 −2.67114.790 1.00 13.28 ATOM 2186 CG MET A 805 27.859 −2.865 15.589 1.00 33.42ATOM 2187 SD MET A 805 28.125 −3.166 17.338 1.00 47.91 ATOM 2188 CE META 805 26.447 −3.244 17.925 1.00 28.62 ATOM 2189 C MET A 805 30.160−2.268 12.542 1.00 11.31 ATOM 2190 O MET A 805 30.761 −1.259 12.908 1.0012.42 ATOM 2191 N ASN A 806 30.530 −2.992 11.490 1.00 11.94 ATOM 2192 CAASN A 806 31.726 −2.673 10.712 1.00 13.21 ATOM 2193 CB ASN A 806 32.537−3.954 10.471 1.00 13.42 ATOM 2194 CG ASN A 806 33.907 −3.676 9.876 1.0016.11 ATOM 2195 OD1 ASN A 806 34.209 −2.549 9.484 1.00 17.92 ATOM 2196ND2 ASN A 806 34.740 −4.706 9.802 1.00 15.54 ATOM 2197 C ASN A 80631.371 −2.023 9.374 1.00 14.20 ATOM 2198 O ASN A 806 30.988 −2.715 8.4301.00 14.08 ATOM 2199 N ARG A 807 31.508 −0.699 9.296 1.00 12.56 ATOM2200 CA ARG A 807 31.189 0.037 8.075 1.00 14.91 ATOM 2201 CB ARG A 80731.410 1.543 8.275 1.00 16.99 ATOM 2202 CG ARG A 807 30.891 2.385 7.1161.00 25.83 ATOM 2203 CD ARG A 807 31.162 3.881 7.280 1.00 30.30 ATOM2204 NE ARG A 807 30.520 4.470 8.457 1.00 20.02 ATOM 2205 CZ ARG A 80731.078 4.525 9.662 1.00 16.27 ATOM 2206 NH1 ARG A 807 32.290 4.025 9.8541.00 20.90 ATOM 2207 NH2 ARG A 807 30.431 5.095 10.670 1.00 15.75 ATOM2208 C ARG A 807 32.021 −0.442 6.889 1.00 13.89 ATOM 2209 O ARG A 80731.573 −0.392 5.736 1.00 13.84 ATOM 2210 N GLU A 808 33.228 −0.910 7.1771.00 11.68 ATOM 2211 CA GLU A 808 34.122 −1.397 6.137 1.00 17.06 ATOM2212 CB GLU A 808 35.502 −1.675 6.731 1.00 16.87 ATOM 2213 CG GLU A 80836.256 −0.394 7.085 1.00 22.64 ATOM 2214 CD GLU A 808 37.556 −0.6457.819 1.00 24.85 ATOM 2215 OE1 GLU A 808 38.293 −1.576 7.430 1.00 26.32ATOM 2216 OE2 GLU A 808 37.846 0.100 8.780 1.00 36.15 ATOM 2217 C GLU A808 33.565 −2.641 5.461 1.00 15.58 ATOM 2218 O GLU A 808 33.929 −2.9564.329 1.00 15.69 ATOM 2219 N LYS A 809 32.677 −3.343 6.156 1.00 14.84ATOM 2220 CA LYS A 809 32.062 −4.544 5.600 1.00 16.67 ATOM 2221 CB LYS A809 32.381 −5.765 6.478 1.00 12.30 ATOM 2222 CG LYS A 809 33.845 −6.1846.405 1.00 13.87 ATOM 2223 CD LYS A 809 34.151 −7.408 7.259 1.00 14.82ATOM 2224 CE LYS A 809 33.430 −8.641 6.745 1.00 25.64 ATOM 2225 NZ LYS A809 33.789 −9.854 7.534 1.00 21.95 ATOM 2226 C LYS A 809 30.555 −4.3635.445 1.00 15.95 ATOM 2227 O LYS A 809 29.770 −5.281 5.693 1.00 18.05ATOM 2228 N LYS A 810 30.156 −3.167 5.022 1.00 15.13 ATOM 2229 CA LYS A810 28.742 −2.867 4.828 1.00 16.24 ATOM 2230 CB LYS A 810 28.549 −1.3834.494 1.00 14.35 ATOM 2231 CG LYS A 810 29.347 −0.869 3.312 1.00 24.48ATOM 2232 CD LYS A 810 29.222 0.647 3.226 1.00 29.64 ATOM 2233 CE LYS A810 29.994 1.224 2.049 1.00 35.68 ATOM 2234 NZ LYS A 810 29.432 0.7860.746 1.00 42.39 ATOM 2235 C LYS A 810 28.139 −3.744 3.734 1.00 14.42ATOM 2236 O LYS A 810 26.921 −3.843 3.607 1.00 14.44 ATOM 2237 N ASN A811 28.995 −4.389 2.950 1.00 13.62 ATOM 2238 CA ASN A 811 28.511 −5.2701.893 1.00 13.60 ATOM 2239 CB ASN A 811 29.680 −5.746 1.016 1.00 18.14ATOM 2240 CG ASN A 811 30.815 −6.340 1.826 1.00 21.65 ATOM 2241 OD1 ASNA 811 30.936 −7.559 1.958 1.00 17.54 ATOM 2242 ND2 ASN A 811 31.651−5.472 2.388 1.00 13.93 ATOM 2243 C ASN A 811 27.777 −6.474 2.487 1.0014.60 ATOM 2244 O ASN A 811 27.084 −7.197 1.777 1.00 13.25 ATOM 2245 NLYS A 812 27.922 −6.677 3.796 1.00 14.05 ATOM 2246 CA LYS A 812 27.279−7.797 4.478 1.00 15.17 ATOM 2247 CB LYS A 812 28.057 −8.150 5.753 1.0015.23 ATOM 2248 CG LYS A 812 29.401 −8.803 5.500 1.00 20.27 ATOM 2249 CDLYS A 812 29.198 −10.137 4.817 1.00 28.44 ATOM 2250 CE LYS A 812 30.497−10.886 4.658 1.00 35.44 ATOM 2251 NZ LYS A 812 30.257 −12.223 4.0481.00 38.51 ATOM 2252 C LYS A 812 25.818 −7.542 4.859 1.00 15.78 ATOM2253 O LYS A 812 25.109 −8.475 5.258 1.00 13.98 ATOM 2254 N ILE A 81325.366 −6.297 4.724 1.00 14.64 ATOM 2255 CA ILE A 813 24.012 −5.9645.144 1.00 14.83 ATOM 2256 CB ILE A 813 23.770 −4.460 5.007 1.00 15.21ATOM 2257 CG2 ILE A 813 22.264 −4.158 5.091 1.00 15.81 ATOM 2258 CG1 ILEA 813 24.616 −3.740 6.073 1.00 13.99 ATOM 2259 CD1 ILE A 813 24.445−2.265 6.070 1.00 27.43 ATOM 2260 C ILE A 813 22.862 −6.792 4.546 1.0014.67 ATOM 2261 O ILE A 813 22.042 −7.309 5.270 1.00 13.44 ATOM 2262 NPRO A 814 22.807 −6.936 3.224 1.00 12.07 ATOM 2263 CD PRO A 814 23.603−6.274 2.191 1.00 14.86 ATOM 2264 CA PRO A 814 21.709 −7.724 2.623 1.0014.39 ATOM 2265 CB PRO A 814 22.060 −7.714 1.152 1.00 13.45 ATOM 2266 CGPRO A 814 22.693 −6.351 1.001 1.00 14.67 ATOM 2267 C PRO A 814 21.605−9.144 3.185 1.00 11.82 ATOM 2268 O PRO A 814 20.525 −9.603 3.570 1.0012.87 ATOM 2269 N SER A 815 22.730 −9.846 3.215 1.00 11.71 ATOM 2270 CASER A 815 22.730 −11.205 3.729 1.00 13.13 ATOM 2271 CB SER A 815 24.102−11.863 3.526 1.00 14.66 ATOM 2272 OG SER A 815 25.124 −11.185 4.2331.00 27.24 ATOM 2273 C SER A 815 22.366 −11.220 5.212 1.00 14.09 ATOM2274 O SER A 815 21.677 −12.120 5.682 1.00 14.61 ATOM 2275 N MET A 81622.809 −10.211 5.937 1.00 14.82 ATOM 2276 CA MET A 816 22.498 −10.1977.353 1.00 14.08 ATOM 2277 CB MET A 816 23.449 −9.254 8.079 1.00 16.95ATOM 2278 CG MET A 816 24.829 −9.872 8.232 1.00 19.08 ATOM 2279 SD MET A816 26.019 −8.905 9.168 1.00 23.16 ATOM 2280 CE MET A 816 25.502 −9.31010.812 1.00 29.41 ATOM 2281 C MET A 816 21.057 −9.838 7.628 1.00 12.78ATOM 2282 O MET A 816 20.477 −10.281 8.613 1.00 13.06 ATOM 2283 N GLN A817 20.464 −9.010 6.765 1.00 11.62 ATOM 2284 CA GLN A 817 19.061 −8.6376.915 1.00 11.33 ATOM 2285 CB GLN A 817 18.666 −7.547 5.899 1.00 12.94ATOM 2286 CG GLN A 817 19.186 −6.179 6.283 1.00 11.95 ATOM 2287 CD GLN A817 18.469 −5.624 7.500 1.00 17.94 ATOM 2288 OE1 GLN A 817 18.544 −6.1838.595 1.00 34.56 ATOM 2289 NE2 GLN A 817 17.759 −4.523 7.309 1.00 34.13ATOM 2290 C GLN A 817 18.202 −9.882 6.714 1.00 13.31 ATOM 2291 O GLN A817 17.254 −10.116 7.472 1.00 10.14 ATOM 2292 N VAL A 818 18.537 −10.6985.715 1.00 12.18 ATOM 2293 CA VAL A 818 17.774 −11.918 5.479 1.00 11.53ATOM 2294 CB VAL A 818 18.252 −12.659 4.210 1.00 13.56 ATOM 2295 CG1 VALA 818 17.500 −13.972 4.063 1.00 10.58 ATOM 2296 CG2 VAL A 818 18.032−11.781 2.982 1.00 17.92 ATOM 2297 C VAL A 818 17.903 −12.858 6.678 1.0011.51 ATOM 2298 O VAL A 818 16.930 −13.494 7.090 1.00 12.55 ATOM 2299 NGLY A 819 19.110 −12.934 7.231 1.00 11.44 ATOM 2300 CA GLY A 819 19.356−13.791 8.376 1.00 12.74 ATOM 2301 C GLY A 819 18.556 −13.335 9.579 1.0013.96 ATOM 2302 O GLY A 819 18.068 −14.149 10.360 1.00 13.49 ATOM 2303 NPHE A 820 18.430 −12.022 9.725 1.00 14.20 ATOM 2304 CA PHE A 820 17.682−11.426 10.825 1.00 11.70 ATOM 2305 CB PHE A 820 17.927 −9.913 10.8331.00 11.32 ATOM 2306 CG PHE A 820 17.122 −9.167 11.858 1.00 9.99 ATOM2307 CD1 PHE A 820 17.268 −9.436 13.209 1.00 23.52 ATOM 2308 CD2 PHE A820 16.225 −8.184 11.466 1.00 17.26 ATOM 2309 CE1 PHE A 820 16.529−8.740 14.151 1.00 19.87 ATOM 2310 CE2 PHE A 820 15.485 −7.488 12.4031.00 16.59 ATOM 2311 CZ PHE A 820 15.640 −7.767 13.746 1.00 17.66 ATOM2312 C PHE A 820 16.191 −11.731 10.651 1.00 12.70 ATOM 2313 O PHE A 82015.498 −12.103 11.604 1.00 10.72 ATOM 2314 N ILE A 821 15.697 −11.5719.429 1.00 10.04 ATOM 2315 CA ILE A 821 14.298 −11.850 9.150 1.00 9.29ATOM 2316 CB ILE A 821 13.957 −11.540 7.679 1.00 10.14 ATOM 2317 CG2 ILEA 821 12.617 −12.166 7.307 1.00 12.87 ATOM 2318 CG1 ILE A 821 13.931−10.022 7.479 1.00 12.03 ATOM 2319 CD1 ILE A 821 13.795 −9.580 6.0371.00 14.77 ATOM 2320 C ILE A 821 13.991 −13.311 9.462 1.00 11.67 ATOM2321 O ILE A 821 13.012 −13.617 10.140 1.00 11.27 ATOM 2322 N ASP A 82214.841 −14.215 8.985 1.00 11.97 ATOM 2323 CA ASP A 822 14.634 −15.6379.237 1.00 14.30 ATOM 2324 CB ASP A 822 15.630 −16.479 8.428 1.00 17.59ATOM 2325 CG ASP A 822 15.317 −16.499 6.942 1.00 17.92 ATOM 2326 OD1 ASPA 822 14.177 −16.153 6.564 1.00 15.98 ATOM 2327 OD2 ASP A 822 16.212−16.880 6.152 1.00 13.97 ATOM 2328 C ASP A 822 14.759 −16.021 10.7141.00 15.42 ATOM 2329 O ASP A 822 13.876 −16.671 11.275 1.00 16.53 ATOM2330 N ALA A 823 15.849 −15.608 11.345 1.00 13.55 ATOM 2331 CA ALA A 82316.101 −15.971 12.737 1.00 15.03 ATOM 2332 CB ALA A 823 17.580 −15.75613.058 1.00 13.84 ATOM 2333 C ALA A 823 15.254 −15.299 13.810 1.00 15.13ATOM 2334 O ALA A 823 14.907 −15.928 14.810 1.00 17.91 ATOM 2335 N ILE A824 14.914 −14.032 13.606 1.00 13.91 ATOM 2336 CA ILE A 824 14.169−13.281 14.611 1.00 14.87 ATOM 2337 CB ILE A 824 14.929 −11.971 14.9661.00 16.51 ATOM 2338 CG2 ILE A 824 14.085 −11.106 15.891 1.00 11.92 ATOM2339 CG1 ILE A 824 16.291 −12.293 15.589 1.00 19.03 ATOM 2340 CD1 ILE A824 16.211 −12.966 16.938 1.00 17.79 ATOM 2341 C ILE A 824 12.736−12.872 14.271 1.00 15.38 ATOM 2342 O ILE A 824 11.817 −13.051 15.0771.00 15.58 ATOM 2343 N CYS A 825 12.548 −12.332 13.074 1.00 11.66 ATOM2344 CA CYS A 825 11.248 −11.798 12.682 1.00 10.83 ATOM 2345 CB CYS A825 11.470 −10.717 11.629 1.00 14.06 ATOM 2346 SG CYS A 825 12.684−9.498 12.156 1.00 12.72 ATOM 2347 C CYS A 825 10.094 −12.685 12.2311.00 12.83 ATOM 2348 O CYS A 825 9.003 −12.606 12.792 1.00 11.78 ATOM2349 N LEU A 826 10.312 −13.508 11.213 1.00 10.64 ATOM 2350 CA LEU A 8269.230 −14.343 10.699 1.00 12.29 ATOM 2351 CB LEU A 826 9.759 −15.2919.621 1.00 17.45 ATOM 2352 CG LEU A 826 10.132 −14.585 8.314 1.00 14.44ATOM 2353 CD1 LEU A 826 10.756 −15.585 7.355 1.00 19.69 ATOM 2354 CD2LEU A 826 8.884 −13.965 7.693 1.00 17.13 ATOM 2355 C LEU A 826 8.428−15.131 11.735 1.00 11.75 ATOM 2356 O LEU A 826 7.194 −15.094 11.7281.00 12.87 ATOM 2357 N GLN A 827 9.115 −15.842 12.620 1.00 9.56 ATOM2358 CA GLN A 827 8.426 −16.637 13.632 1.00 10.96 ATOM 2359 CB GLN A 8279.438 −17.368 14.507 1.00 9.95 ATOM 2360 CG GLN A 827 10.207 −18.46513.805 1.00 14.60 ATOM 2361 CD GLN A 827 11.365 −18.949 14.646 1.0027.21 ATOM 2362 OE1 GLN A 827 12.420 −18.312 14.695 1.00 20.68 ATOM 2363NE2 GLN A 827 11.169 −20.068 15.335 1.00 24.19 ATOM 2364 C GLN A 8277.516 −15.798 14.524 1.00 13.14 ATOM 2365 O GLN A 827 6.428 −16.23514.906 1.00 13.21 ATOM 2366 N LEU A 828 7.966 −14.596 14.862 1.00 10.02ATOM 2367 CA LEU A 828 7.182 −13.713 15.720 1.00 10.78 ATOM 2368 CB LEUA 828 8.037 −12.521 16.166 1.00 9.67 ATOM 2369 CG LEU A 828 7.315−11.431 16.966 1.00 14.41 ATOM 2370 CD1 LEU A 828 6.653 −12.048 18.1851.00 16.13 ATOM 2371 CD2 LEU A 828 8.300 −10.351 17.389 1.00 14.03 ATOM2372 C LEU A 828 5.902 −13.218 15.036 1.00 11.55 ATOM 2373 O LEU A 8284.814 −13.290 15.609 1.00 12.50 ATOM 2374 N TYR A 829 6.024 −12.71713.812 1.00 10.38 ATOM 2375 CA TYR A 829 4.851 −12.217 13.109 1.00 11.38ATOM 2376 CB TYR A 829 5.286 −11.392 11.892 1.00 9.07 ATOM 2377 CG TYR A829 5.967 −10.112 12.324 1.00 13.32 ATOM 2378 CD1 TYR A 829 5.298 −9.18913.118 1.00 8.62 ATOM 2379 CE1 TYR A 829 5.926 −8.037 13.569 1.00 10.58ATOM 2380 CD2 TYR A 829 7.290 −9.849 11.989 1.00 10.78 ATOM 2381 CE2 TYRA 829 7.930 −8.699 12.440 1.00 8.02 ATOM 2382 CZ TYR A 829 7.241 −7.80013.228 1.00 8.64 ATOM 2383 OH TYR A 829 7.867 −6.659 13.688 1.00 10.63ATOM 2384 C TYR A 829 3.908 −13.349 12.731 1.00 12.07 ATOM 2385 O TYR A829 2.704 −13.140 12.594 1.00 14.07 ATOM 2386 N GLU A 830 4.452 −14.55512.585 1.00 14.19 ATOM 2387 CA GLU A 830 3.614 −15.709 12.274 1.00 14.53ATOM 2388 CB GLU A 830 4.469 −16.919 11.881 1.00 15.21 ATOM 2389 CG GLUA 830 5.196 −16.751 10.557 1.00 18.48 ATOM 2390 CD GLU A 830 6.057−17.948 10.208 1.00 27.35 ATOM 2391 OE1 GLU A 830 6.422 −18.701 11.1331.00 25.55 ATOM 2392 OE2 GLU A 830 6.380 −18.127 9.014 1.00 25.64 ATOM2393 C GLU A 830 2.806 −16.027 13.531 1.00 15.34 ATOM 2394 O GLU A 8301.594 −16.245 13.462 1.00 15.05 ATOM 2395 N ALA A 831 3.484 −16.03714.679 1.00 12.88 ATOM 2396 CA ALA A 831 2.836 −16.319 15.958 1.00 13.60ATOM 2397 CB ALA A 831 3.877 −16.341 17.080 1.00 14.75 ATOM 2398 C ALA A831 1.764 −15.279 16.264 1.00 14.36 ATOM 2399 O ALA A 831 0.666 −15.61716.714 1.00 13.70 ATOM 2400 N LEU A 832 2.085 −14.010 16.026 1.00 11.70ATOM 2401 CA LEU A 832 1.135 −12.935 16.276 1.00 12.90 ATOM 2402 CB LEUA 832 1.800 −11.577 16.030 1.00 12.02 ATOM 2403 CG LEU A 832 0.935−10.334 16.256 1.00 13.07 ATOM 2404 CD1 LEU A 832 0.367 −10.354 17.6701.00 16.97 ATOM 2405 CD2 LEU A 832 1.764 −9.076 16.018 1.00 12.70 ATOM2406 C LEU A 832 −0.093 −13.098 15.382 1.00 13.07 ATOM 2407 O LEU A 832−1.221 −12.851 15.811 1.00 12.63 ATOM 2408 N THR A 833 0.125 −13.52214.140 1.00 10.33 ATOM 2409 CA THR A 833 −0.985 −13.720 13.213 1.0011.65 ATOM 2410 CB THR A 833 −0.471 −14.019 11.798 1.00 15.54 ATOM 2411OG1 THR A 833 0.250 −12.881 11.309 1.00 13.44 ATOM 2412 CG2 THR A 833−1.631 −14.319 10.856 1.00 20.09 ATOM 2413 C THR A 833 −1.856 −14.87513.709 1.00 13.24 ATOM 2414 O THR A 833 −3.070 −14.879 13.512 1.00 14.62ATOM 2415 N HIS A 834 −1.233 −15.855 14.358 1.00 12.04 ATOM 2416 CA HISA 834 −1.974 −16.988 14.901 1.00 15.35 ATOM 2417 CB HIS A 834 −1.010−18.045 15.451 1.00 17.31 ATOM 2418 CG HIS A 834 −1.686 −19.161 16.1741.00 21.70 ATOM 2419 CD2 HIS A 834 −2.005 −20.422 15.792 1.00 27.35 ATOM2420 ND1 HIS A 834 −2.158 −19.040 17.471 1.00 27.23 ATOM 2421 CE1 HIS A834 −2.728 −20.162 17.843 1.00 22.73 ATOM 2422 NE2 HIS A 834 −2.650−21.026 16.836 1.00 26.03 ATOM 2423 C HIS A 834 −2.907 −16.495 16.0111.00 16.43 ATOM 2424 O HIS A 834 −4.061 −16.917 16.101 1.00 16.32 ATOM2425 N VAL A 835 −2.402 −15.600 16.852 1.00 14.39 ATOM 2426 CA VAL A 835−3.201 −15.042 17.940 1.00 16.17 ATOM 2427 CB VAL A 835 −2.329 −14.17718.879 1.00 20.06 ATOM 2428 CG1 VAL A 835 −3.203 −13.433 19.878 1.0026.18 ATOM 2429 CG2 VAL A 835 −1.336 −15.067 19.616 1.00 22.85 ATOM 2430C VAL A 835 −4.345 −14.196 17.376 1.00 18.30 ATOM 2431 O VAL A 835−5.462 −14.219 17.899 1.00 16.68 ATOM 2432 N SER A 836 −4.061 −13.46116.302 1.00 15.55 ATOM 2433 CA SER A 836 −5.060 −12.620 15.646 1.0015.62 ATOM 2434 CB SER A 836 −5.081 −11.222 16.267 1.00 18.44 ATOM 2435OG SER A 836 −6.092 −10.430 15.665 1.00 24.05 ATOM 2436 C SER A 836−4.744 −12.516 14.153 1.00 15.03 ATOM 2437 O SER A 836 −3.754 −11.90113.759 1.00 14.82 ATOM 2438 N GLU A 837 −5.596 −13.123 13.334 1.00 16.29ATOM 2439 CA GLU A 837 −5.423 −13.139 11.886 1.00 16.40 ATOM 2440 CB GLUA 837 −6.578 −13.922 11.244 1.00 19.29 ATOM 2441 CG GLU A 837 −6.524−14.017 9.722 1.00 30.56 ATOM 2442 CD GLU A 837 −5.259 −14.685 9.2131.00 40.78 ATOM 2443 OE1 GLU A 837 −4.925 −15.785 9.704 1.00 33.63 ATOM2444 OE2 GLU A 837 −4.603 −14.112 8.316 1.00 45.55 ATOM 2445 C GLU A 837−5.324 −11.749 11.256 1.00 14.00 ATOM 2446 O GLU A 837 −4.672 −11.57410.227 1.00 16.56 ATOM 2447 N ASP A 838 −5.967 −10.762 11.871 1.00 14.38ATOM 2448 CA ASP A 838 −5.938 −9.402 11.349 1.00 12.78 ATOM 2449 CB ASPA 838 −6.990 −8.547 12.060 1.00 12.80 ATOM 2450 CG ASP A 838 −8.410−8.929 11.669 1.00 31.66 ATOM 2451 OD1 ASP A 838 −8.770 −8.750 10.4871.00 25.15 ATOM 2452 OD2 ASP A 838 −9.162 −9.414 12.540 1.00 29.94 ATOM2453 C ASP A 838 −4.558 −8.751 11.468 1.00 11.81 ATOM 2454 O ASP A 838−4.355 −7.625 11.017 1.00 12.87 ATOM 2455 N CYS A 839 −3.610 −9.45612.080 1.00 14.34 ATOM 2456 CA CYS A 839 −2.254 −8.929 12.203 1.00 14.23ATOM 2457 CB CYS A 839 −1.619 −9.354 13.533 1.00 12.27 ATOM 2458 SG CYSA 839 −2.115 −8.349 14.969 1.00 12.53 ATOM 2459 C CYS A 839 −1.412−9.440 11.038 1.00 15.74 ATOM 2460 O CYS A 839 −0.222 −9.142 10.941 1.0013.52 ATOM 2461 N PHE A 840 −2.044 −10.209 10.152 1.00 14.15 ATOM 2462CA PHE A 840 −1.364 −10.765 8.983 1.00 14.85 ATOM 2463 CB PHE A 840−2.370 −11.451 8.052 1.00 18.01 ATOM 2464 CG PHE A 840 −1.760 −11.9266.764 1.00 16.92 ATOM 2465 CD1 PHE A 840 −0.886 −13.001 6.751 1.00 13.52ATOM 2466 CD2 PHE A 840 −2.010 −11.257 5.575 1.00 19.38 ATOM 2467 CE1PHE A 840 −0.269 −13.398 5.575 1.00 23.30 ATOM 2468 CE2 PHE A 840 −1.397−11.649 4.396 1.00 23.75 ATOM 2469 CZ PHE A 840 −0.525 −12.720 4.3971.00 22.76 ATOM 2470 C PHE A 840 −0.541 −9.768 8.155 1.00 13.70 ATOM2471 O PHE A 840 0.546 −10.105 7.678 1.00 13.33 ATOM 2472 N PRO A 841−1.049 −8.537 7.958 1.00 12.97 ATOM 2473 CD PRO A 841 −2.369 −8.0028.339 1.00 14.47 ATOM 2474 CA PRO A 841 −0.294 −7.557 7.168 1.00 12.84ATOM 2475 CB PRO A 841 −1.127 −6.287 7.312 1.00 14.37 ATOM 2476 CG PRO A841 −2.533 −6.826 7.391 1.00 14.58 ATOM 2477 C PRO A 841 1.151 −7.3677.630 1.00 14.54 ATOM 2478 O PRO A 841 2.034 −7.065 6.826 1.00 13.75ATOM 2479 N LEU A 842 1.393 −7.530 8.926 1.00 11.66 ATOM 2480 CA LEU A842 2.747 −7.384 9.444 1.00 12.35 ATOM 2481 CB LEU A 842 2.732 −7.43010.977 1.00 11.85 ATOM 2482 CG LEU A 842 2.039 −6.228 11.624 1.00 12.78ATOM 2483 CD1 LEU A 842 1.900 −6.434 13.131 1.00 14.23 ATOM 2484 CD2 LEUA 842 2.837 −4.975 11.321 1.00 14.25 ATOM 2485 C LEU A 842 3.613 −8.5138.880 1.00 13.95 ATOM 2486 O LEU A 842 4.741 −8.290 8.444 1.00 13.84ATOM 2487 N LEU A 843 3.067 −9.727 8.882 1.00 11.90 ATOM 2488 CA LEU A843 3.779 −10.889 8.359 1.00 11.64 ATOM 2489 CB LEU A 843 2.995 −12.1618.670 1.00 10.07 ATOM 2490 CG LEU A 843 3.532 −13.468 8.084 1.00 9.50ATOM 2491 CD1 LEU A 843 4.940 −13.735 8.588 1.00 13.64 ATOM 2492 CD2 LEUA 843 2.597 −14.608 8.466 1.00 12.37 ATOM 2493 C LEU A 843 3.971 −10.7516.847 1.00 11.74 ATOM 2494 O LEU A 843 5.054 −11.003 6.319 1.00 13.14ATOM 2495 N ASP A 844 2.909 −10.342 6.160 1.00 13.31 ATOM 2496 CA ASP A844 2.943 −10.154 4.711 1.00 14.45 ATOM 2497 CB ASP A 844 1.573 −9.6394.245 1.00 18.19 ATOM 2498 CG ASP A 844 1.354 −9.771 2.739 1.00 13.51ATOM 2499 OD1 ASP A 844 2.141 −10.459 2.057 1.00 18.86 ATOM 2500 OD2 ASPA 844 0.367 −9.187 2.243 1.00 17.91 ATOM 2501 C ASP A 844 4.053 −9.1534.366 1.00 13.87 ATOM 2502 O ASP A 844 4.854 −9.386 3.460 1.00 13.07ATOM 2503 N GLY A 845 4.100 −8.046 5.104 1.00 12.67 ATOM 2504 CA GLY A845 5.115 −7.035 4.862 1.00 11.69 ATOM 2505 C GLY A 845 6.529 −7.5405.097 1.00 11.05 ATOM 2506 O GLY A 845 7.447 −7.240 4.330 1.00 12.51ATOM 2507 N CYS A 846 6.704 −8.314 6.161 1.00 10.28 ATOM 2508 CA CYS A846 8.005 −8.882 6.507 1.00 10.93 ATOM 2509 CB CYS A 846 7.889 −9.6437.831 1.00 14.58 ATOM 2510 SG CYS A 846 9.443 −10.273 8.485 1.00 12.82ATOM 2511 C CYS A 846 8.497 −9.821 5.398 1.00 11.92 ATOM 2512 O CYS A846 9.661 −9.762 4.985 1.00 11.24 ATOM 2513 N ARG A 847 7.605 −10.6834.914 1.00 12.77 ATOM 2514 CA ARG A 847 7.953 −11.618 3.853 1.00 13.72ATOM 2515 CB ARG A 847 6.762 −12.527 3.535 1.00 11.63 ATOM 2516 CG ARG A847 6.457 −13.545 4.619 1.00 13.10 ATOM 2517 CD ARG A 847 5.180 −14.3084.316 1.00 17.35 ATOM 2518 NE ARG A 847 4.978 −15.402 5.262 1.00 19.23ATOM 2519 CZ ARG A 847 3.840 −16.077 5.389 1.00 21.47 ATOM 2520 NH1 ARGA 847 2.796 −15.769 4.632 1.00 24.29 ATOM 2521 NH2 ARG A 847 3.750−17.059 6.275 1.00 27.21 ATOM 2522 C ARG A 847 8.371 −10.870 2.592 1.0013.53 ATOM 2523 O ARG A 847 9.320 −11.265 1.906 1.00 13.20 ATOM 2524 NLYS A 848 7.659 −9.793 2.283 1.00 12.35 ATOM 2525 CA LYS A 848 7.977−9.007 1.099 1.00 14.65 ATOM 2526 CB LYS A 848 6.925 −7.915 0.880 1.0016.22 ATOM 2527 CG LYS A 848 5.567 −8.447 0.413 1.00 14.77 ATOM 2528 CDLYS A 848 4.579 −7.308 0.195 1.00 19.65 ATOM 2529 CE LYS A 848 3.210−7.817 −0.206 1.00 19.42 ATOM 2530 NZ LYS A 848 2.214 −6.709 −0.212 1.0023.11 ATOM 2531 C LYS A 848 9.364 −8.392 1.229 1.00 14.80 ATOM 2532 OLYS A 848 10.112 −8.319 0.253 1.00 13.12 ATOM 2533 N ASN A 849 9.713−7.953 2.435 1.00 13.42 ATOM 2534 CA ASN A 849 11.034 −7.369 2.648 1.0013.07 ATOM 2535 CB ASN A 849 11.086 −6.646 3.995 1.00 13.67 ATOM 2536 CGASN A 849 10.412 −5.288 3.950 1.00 17.85 ATOM 2537 OD1 ASN A 849 9.863−4.821 4.949 1.00 16.87 ATOM 2538 ND2 ASN A 849 10.461 −4.638 2.790 1.0013.21 ATOM 2539 C ASN A 849 12.122 −8.434 2.568 1.00 12.00 ATOM 2540 OASN A 849 13.252 −8.148 2.165 1.00 11.88 ATOM 2541 N ARG A 850 11.797−9.667 2.945 1.00 11.53 ATOM 2542 CA ARG A 850 12.793 −10.729 2.860 1.0011.98 ATOM 2543 CB ARG A 850 12.285 −12.037 3.473 1.00 14.13 ATOM 2544CG ARG A 850 13.373 −13.110 3.508 1.00 13.55 ATOM 2545 CD ARG A 85012.838 −14.511 3.781 1.00 18.02 ATOM 2546 NE ARG A 850 13.930 −15.4574.001 1.00 16.95 ATOM 2547 CZ ARG A 850 14.743 −15.919 3.052 1.00 14.40ATOM 2548 NH1 ARG A 850 14.595 −15.533 1.790 1.00 16.03 ATOM 2549 NH2ARG A 850 15.727 −16.754 3.373 1.00 12.51 ATOM 2550 C ARG A 850 13.138−10.972 1.399 1.00 13.81 ATOM 2551 O ARG A 850 14.304 −11.151 1.054 1.0015.14 ATOM 2552 N GLN A 851 12.118 −10.985 0.542 1.00 16.03 ATOM 2553 CAGLN A 851 12.317 −11.193 −0.892 1.00 15.42 ATOM 2554 CB GLN A 851 10.969−11.156 −1.622 1.00 17.30 ATOM 2555 CG GLN A 851 11.039 −11.399 −3.1271.00 30.46 ATOM 2556 CD GLN A 851 11.475 −10.174 −3.912 1.00 34.81 ATOM2557 OE1 GLN A 851 10.862 −9.110 −3.814 1.00 37.41 ATOM 2558 NE2 GLN A851 12.534 −10.320 −4.704 1.00 40.89 ATOM 2559 C GLN A 851 13.229−10.109 −1.436 1.00 16.49 ATOM 2560 O GLN A 851 14.151 −10.371 −2.2081.00 15.70 ATOM 2561 N LYS A 852 12.953 −8.867 −1.014 1.00 15.86 ATOM2562 CA LYS A 852 13.705 −7.685 −1.428 1.00 16.63 ATOM 2563 CB LYS A 85213.065 −6.405 −0.838 1.00 13.58 ATOM 2564 CG LYS A 852 11.802 −6.008−1.561 1.00 18.37 ATOM 2565 CD LYS A 852 12.183 −5.582 −2.958 1.00 31.95ATOM 2566 CE LYS A 852 11.002 −5.087 −3.751 1.00 37.83 ATOM 2567 NZ LYSA 852 11.421 −4.599 −5.099 1.00 41.92 ATOM 2568 C LYS A 852 15.175−7.754 −1.037 1.00 15.46 ATOM 2569 O LYS A 852 16.055 −7.542 −1.874 1.0014.58 ATOM 2570 N TRP A 853 15.446 −8.063 0.225 1.00 12.99 ATOM 2571 CATRP A 853 16.821 −8.168 0.705 1.00 12.72 ATOM 2572 CB TRP A 853 16.843−8.299 2.228 1.00 11.94 ATOM 2573 CG TRP A 853 16.640 −7.011 2.957 1.0011.40 ATOM 2574 CD2 TRP A 853 17.485 −5.864 2.913 1.00 14.74 ATOM 2575CE2 TRP A 853 16.929 −4.888 3.763 1.00 12.41 ATOM 2576 CE3 TRP A 85318.675 −5.554 2.236 1.00 10.90 ATOM 2577 CD1 TRP A 853 15.618 −6.7013.813 1.00 11.02 ATOM 2578 NE1 TRP A 853 15.781 −5.429 4.303 1.00 14.15ATOM 2579 CZ2 TRP A 853 17.502 −3.638 3.958 1.00 12.03 ATOM 2580 CZ3 TRPA 853 19.246 −4.312 2.427 1.00 13.77 ATOM 2581 CH2 TRP A 853 18.663−3.370 3.280 1.00 16.08 ATOM 2582 C TRP A 853 17.543 −9.357 0.074 1.0013.55 ATOM 2583 O TRP A 853 18.722 −9.265 −0.282 1.00 13.19 ATOM 2584 NGLN A 854 16.836 −10.472 −0.062 1.00 12.06 ATOM 2585 CA GLN A 854 17.427−11.667 −0.657 1.00 13.49 ATOM 2586 CB GLN A 854 16.426 −12.822 −0.6301.00 13.86 ATOM 2587 CG GLN A 854 16.934 −14.128 −1.242 1.00 15.91 ATOM2588 CD GLN A 854 18.267 −14.585 −0.665 1.00 23.66 ATOM 2589 OE1 GLN A854 18.544 −14.404 0.520 1.00 20.44 ATOM 2590 NE2 GLN A 854 19.091−15.199 −1.504 1.00 26.84 ATOM 2591 C GLN A 854 17.869 −11.400 −2.0941.00 13.14 ATOM 2592 O GLN A 854 18.920 −11.880 −2.524 1.00 15.55 ATOM2593 N ALA A 855 17.069 −10.635 −2.832 1.00 14.63 ATOM 2594 CA ALA A 85517.408 −10.318 −4.219 1.00 15.08 ATOM 2595 CB ALA A 855 16.264 −9.563−4.884 1.00 17.06 ATOM 2596 C ALA A 855 18.697 −9.504 −4.303 1.00 16.23ATOM 2597 O ALA A 855 19.439 −9.611 −5.278 1.00 17.06 ATOM 2598 N LEU A856 18.959 −8.689 −3.287 1.00 15.11 ATOM 2599 CA LEU A 856 20.178 −7.889−3.261 1.00 17.23 ATOM 2600 CB LEU A 856 20.031 −6.715 −2.284 1.00 11.53ATOM 2601 CG LEU A 856 18.968 −5.676 −2.643 1.00 15.60 ATOM 2602 CD1 LEUA 856 18.996 −4.549 −1.634 1.00 19.73 ATOM 2603 CD2 LEU A 856 19.226−5.145 −4.047 1.00 12.95 ATOM 2604 C LEU A 856 21.362 −8.754 −2.835 1.0017.35 ATOM 2605 O LEU A 856 22.478 −8.601 −3.337 1.00 17.30 ATOM 2606 NALA A 857 21.109 −9.674 −1.911 1.00 16.52 ATOM 2607 CA ALA A 857 22.156−10.545 −1.396 1.00 17.82 ATOM 2608 CB ALA A 857 21.708 −11.155 −0.0791.00 15.78 ATOM 2609 C ALA A 857 22.616 −11.651 −2.339 1.00 19.95 ATOM2610 O ALA A 857 23.781 −12.048 −2.305 1.00 21.30 ATOM 2611 N GLU A 85821.715 −12.144 −3.181 1.00 19.75 ATOM 2612 CA GLU A 858 22.059 −13.233−4.091 1.00 23.14 ATOM 2613 CB GLU A 858 20.798 −14.008 −4.475 1.0028.23 ATOM 2614 CG GLU A 858 19.735 −13.155 −5.139 1.00 35.46 ATOM 2615CD GLU A 858 18.516 −13.957 −5.548 1.00 41.30 ATOM 2616 OE1 GLU A 85817.928 −14.635 −4.679 1.00 46.06 ATOM 2617 OE2 GLU A 858 18.144 −13.905−6.739 1.00 53.40 ATOM 2618 C GLU A 858 22.773 −12.775 −5.356 1.00 24.66ATOM 2619 O GLU A 858 22.769 −11.561 −5.640 1.00 27.06 ATOM 2620 OXT GLUA 858 23.319 −13.654 −6.053 1.00 33.90 TER 2621 GLU A 858 ATOM 2622 OHOH W 1 14.659 12.373 18.930 1.00 11.90 ATOM 2623 O HOH W 2 9.029 0.61615.467 1.00 15.60 ATOM 2624 O HOH W 3 17.339 −0.310 24.269 1.00 9.87ATOM 2625 O HOH W 4 17.787 8.492 22.312 1.00 9.91 ATOM 2626 O HOH W 522.322 0.101 41.405 1.00 10.58 ATOM 2627 O HOH W 6 7.037 −4.929 2.9381.00 15.52 ATOM 2628 O HOH W 7 24.844 0.942 17.890 1.00 12.19 ATOM 2629O HOH W 8 17.812 −5.285 21.940 1.00 13.09 ATOM 2630 O HOH W 9 19.355−1.244 21.749 1.00 11.09 ATOM 2631 O HOH W 10 11.998 −15.929 13.123 1.0015.08 ATOM 2632 O HOH W 11 17.595 6.868 5.858 1.00 17.40 ATOM 2633 O HOHW 12 20.522 −8.124 28.490 1.00 16.30 ATOM 2634 O HOH W 13 7.122 8.42630.706 1.00 12.74 ATOM 2635 O HOH W 14 14.281 −0.736 24.882 1.00 10.20ATOM 2636 O HOH W 15 27.778 −4.812 7.714 1.00 14.34 ATOM 2637 O HOH W 1645.697 −5.856 19.373 1.00 13.79 ATOM 2638 O HOH W 17 32.028 0.851 11.8591.00 12.49 ATOM 2639 O HOH W 18 12.716 −7.833 22.260 1.00 11.62 ATOM2640 O HOH W 19 20.770 −7.019 24.953 1.00 13.66 ATOM 2641 O HOH W 209.679 −8.387 30.457 1.00 18.04 ATOM 2642 O HOH W 21 20.996 −1.566 19.5841.00 15.27 ATOM 2643 O HOH W 22 5.367 −8.570 29.548 1.00 17.36 ATOM 2644O HOH W 23 25.138 −9.337 1.725 1.00 17.63 ATOM 2645 O HOH W 24 −9.020−0.116 43.708 1.00 15.91 ATOM 2646 O HOH W 25 22.657 −6.174 29.194 1.0017.18 ATOM 2647 O HOH W 26 −4.280 19.557 21.192 1.00 19.85 ATOM 2648 OHOH W 27 14.289 6.604 13.852 1.00 14.85 ATOM 2649 O HOH W 28 11.411−1.302 13.935 1.00 12.80 ATOM 2650 O HOH W 29 11.700 13.882 15.200 1.0014.97 ATOM 2651 O HOH W 30 18.410 10.076 12.196 1.00 19.59 ATOM 2652 OHOH W 31 26.709 7.571 23.378 1.00 17.44 ATOM 2653 O HOH W 32 25.4205.805 17.773 1.00 17.40 ATOM 2654 O HOH W 33 11.087 10.589 10.070 1.0017.81 ATOM 2655 O HOH W 34 11.500 −19.954 26.231 1.00 16.07 ATOM 2656 OHOH W 35 −5.204 −5.042 34.106 1.00 17.24 ATOM 2657 O HOH W 36 1.9419.940 36.428 1.00 13.95 ATOM 2658 O HOH W 37 23.916 7.238 15.924 1.0014.00 ATOM 2659 O HOH W 38 4.522 21.473 19.911 1.00 20.60 ATOM 2660 OHOH W 39 7.654 32.374 24.586 1.00 19.77 ATOM 2661 O HOH W 40 −11.1058.617 12.732 1.00 20.19 ATOM 2662 O HOH W 41 14.266 14.289 20.855 1.0016.50 ATOM 2663 O HOH W 42 27.797 −9.140 13.072 1.00 17.28 ATOM 2664 OHOH W 43 13.361 −5.781 20.636 1.00 17.62 ATOM 2665 O HOH W 44 9.43917.952 22.920 1.00 20.34 ATOM 2666 O HOH W 45 13.506 −19.339 23.851 1.0017.51 ATOM 2667 O HOH W 46 −9.608 −2.484 44.794 1.00 18.03 ATOM 2668 OHOH W 47 19.179 −3.517 23.479 1.00 14.63 ATOM 2669 O HOH W 48 20.825−1.771 7.357 1.00 15.56 ATOM 2670 O HOH W 49 3.953 −2.401 8.103 1.0015.98 ATOM 2671 O HOH W 50 5.164 2.828 12.389 1.00 17.57 ATOM 2672 O HOHW 51 22.475 −6.004 8.390 1.00 20.31 ATOM 2673 O HOH W 52 −1.505 −7.7133.922 1.00 20.93 ATOM 2674 O HOH W 53 16.030 13.344 15.066 1.00 22.86ATOM 2675 O HOH W 54 3.120 33.114 17.327 1.00 18.81 ATOM 2676 O HOH W 556.517 19.676 19.112 1.00 20.43 ATOM 2677 O HOH W 56 27.812 5.941 11.2691.00 19.39 ATOM 2678 O HOH W 57 14.704 9.138 12.638 1.00 17.37 ATOM 2679O HOH W 58 10.813 −19.129 28.734 1.00 23.50 ATOM 2680 O HOH W 59 9.603−13.958 1.403 1.00 20.05 ATOM 2681 O HOH W 60 46.209 −3.550 17.835 1.0018.22 ATOM 2682 O HOH W 61 24.760 −2.396 10.006 1.00 20.80 ATOM 2683 OHOH W 62 11.077 3.087 12.585 1.00 21.05 ATOM 2684 O HOH W 63 10.534−10.726 28.998 1.00 21.18 ATOM 2685 O HOH W 64 −0.961 −11.064 33.4401.00 18.63 ATOM 2686 O HOH W 65 20.890 0.577 15.388 1.00 19.77 ATOM 2687O HOH W 66 21.685 13.866 20.281 1.00 24.54 ATOM 2688 O HOH W 67 −5.012−3.878 8.180 1.00 21.24 ATOM 2689 O HOH W 68 −10.443 9.371 15.194 1.0019.03 ATOM 2690 O HOH W 69 26.635 8.578 39.152 1.00 19.48 ATOM 2691 OHOH W 70 21.837 −4.044 23.094 1.00 14.46 ATOM 2692 O HOH W 71 18.9790.534 3.275 1.00 19.32 ATOM 2693 O HOH W 72 −7.687 −4.529 35.484 1.0019.76 ATOM 2694 O HOH W 73 −4.441 9.972 35.483 1.00 21.75 ATOM 2695 OHOH W 74 22.147 0.611 18.233 1.00 21.06 ATOM 2696 O HOH W 75 25.6257.694 19.834 1.00 17.79 ATOM 2697 O HOH W 76 −9.716 14.941 11.027 1.0020.22 ATOM 2698 O HOH W 77 14.015 −1.710 16.866 1.00 19.03 ATOM 2699 OHOH W 78 21.861 −3.953 20.354 1.00 17.68 ATOM 2700 O HOH W 79 21.854−11.471 10.659 1.00 21.05 ATOM 2701 O HOH W 80 15.795 −5.944 −4.295 1.0017.34 ATOM 2702 O HOH W 81 26.427 −5.333 20.748 1.00 28.65 ATOM 2703 OHOH W 82 0.806 16.637 36.547 1.00 22.11 ATOM 2704 O HOH W 83 28.8835.909 33.300 1.00 35.99 ATOM 2705 O HOH W 84 0.615 −5.836 36.804 1.0021.63 ATOM 2706 O HOH W 85 14.416 −12.696 −3.692 1.00 22.36 ATOM 2707 OHOH W 86 −4.841 7.644 43.980 1.00 19.92 ATOM 2708 O HOH W 87 −6.0595.564 10.293 1.00 22.49 ATOM 2709 O HOH W 88 7.210 1.031 13.002 1.0019.78 ATOM 2710 O HOH W 89 −5.786 −6.329 9.023 1.00 20.32 ATOM 2711 OHOH W 90 19.117 4.909 35.027 1.00 17.30 ATOM 2712 O HOH W 91 10.59213.017 38.293 1.00 23.66 ATOM 2713 O HOH W 92 −9.801 5.234 16.132 1.0020.64 ATOM 2714 O HOH W 93 −6.370 −17.172 24.540 1.00 23.65 ATOM 2715 OHOH W 94 −6.833 1.342 45.207 1.00 17.92 ATOM 2716 O HOH W 95 33.715−7.279 11.000 1.00 17.67 ATOM 2717 O HOH W 96 5.722 31.659 29.252 1.0019.35 ATOM 2718 O HOH W 97 14.155 −2.890 10.083 1.00 16.30 ATOM 2719 OHOH W 98 19.709 −5.898 20.414 1.00 27.45 ATOM 2720 O HOH W 99 4.418−3.958 2.629 1.00 23.70 ATOM 2721 O HOH W 100 5.739 5.419 41.566 1.0026.30 ATOM 2722 O HOH W 101 1.882 −10.334 12.547 1.00 21.56 ATOM 2723 OHOH W 102 1.506 9.558 7.516 1.00 21.76 ATOM 2724 O HOH W 103 23.2111.757 4.698 1.00 23.21 ATOM 2725 O HOH W 104 36.282 2.363 9.440 1.0027.13 ATOM 2726 O HOH W 105 27.600 −11.267 2.472 1.00 18.59 ATOM 2727 OHOH W 106 16.305 16.757 22.862 1.00 25.14 ATOM 2728 O HOH W 107 21.223−0.443 4.807 1.00 20.51 ATOM 2729 O HOH W 108 12.939 13.840 12.680 1.0026.10 ATOM 2730 O HOH W 109 10.191 −9.652 24.549 1.00 17.97 ATOM 2731 OHOH W 110 9.527 −19.990 11.160 1.00 34.52 ATOM 2732 O HOH W 111 2.300−4.117 6.982 1.00 21.40 ATOM 2733 O HOH W 112 31.807 5.599 25.384 1.0019.28 ATOM 2734 O HOH W 113 11.858 5.625 12.858 1.00 18.80 ATOM 2735 OHOH W 114 2.975 3.851 3.583 1.00 28.02 ATOM 2736 O HOH W 115 22.328−3.325 9.278 1.00 18.13 ATOM 2737 O HOH W 116 7.581 21.278 17.210 1.0026.33 ATOM 2738 O HOH W 117 −8.959 18.330 19.702 1.00 25.41 ATOM 2739 OHOH W 118 −7.913 −3.625 46.688 1.00 16.16 ATOM 2740 O HOH W 119 29.369−4.122 35.016 1.00 21.35 ATOM 2741 O HOH W 120 −10.313 4.301 39.676 1.0020.84 ATOM 2742 O HOH W 121 36.288 −8.163 10.383 1.00 29.41 ATOM 2743 OHOH W 122 −5.305 0.154 7.066 1.00 32.03 ATOM 2744 O HOH W 123 15.8929.345 6.948 1.00 31.98 ATOM 2745 O HOH W 124 −7.934 −11.981 26.594 1.0024.88 ATOM 2746 O HOH W 125 −7.700 −14.762 14.417 1.00 27.16 ATOM 2747 OHOH W 126 7.924 19.345 32.073 1.00 27.10 ATOM 2748 O HOH W 127 22.963−15.271 −0.194 1.00 34.57 ATOM 2749 O HOH W 128 14.018 4.418 0.344 1.0027.94 ATOM 2750 O HOH W 129 13.334 16.377 17.301 1.00 27.05 ATOM 2751 OHOH W 130 30.641 −11.391 0.176 1.00 21.79 ATOM 2752 O HOH W 131 −5.143−9.116 6.397 1.00 26.22 ATOM 2753 O HOH W 132 44.452 2.118 22.189 1.0025.35 ATOM 2754 O HOH W 133 −0.942 −8.268 32.526 1.00 21.73 ATOM 2755 OHOH W 134 32.286 8.100 17.531 1.00 30.18 ATOM 2756 O HOH W 135 4.471−22.268 17.254 1.00 22.18 ATOM 2757 O HOH W 136 20.964 −7.154 10.0511.00 23.34 ATOM 2758 O HOH W 137 −6.984 26.107 22.746 1.00 26.33 ATOM2759 O HOH W 138 17.856 14.348 24.807 1.00 20.33 ATOM 2760 O HOH W 13910.038 −5.546 41.193 1.00 26.62 ATOM 2761 O HOH W 140 13.989 13.83716.687 1.00 27.53 ATOM 2762 O HOH W 141 23.629 −13.084 9.502 1.00 28.21ATOM 2763 O HOH W 142 31.635 7.713 14.307 1.00 30.30 ATOM 2764 O HOH W143 6.811 −2.344 −0.868 1.00 24.47 ATOM 2765 O HOH W 144 7.278 −9.98130.756 1.00 27.03 ATOM 2766 O HOH W 145 −6.981 7.089 6.281 1.00 26.94ATOM 2767 O HOH W 146 −8.635 18.558 29.861 1.00 27.91 ATOM 2768 O HOH W147 30.525 −1.680 34.334 1.00 24.09 ATOM 2769 O HOH W 148 2.251 −13.8672.121 1.00 25.49 ATOM 2770 O HOH W 149 −8.063 −9.740 29.191 1.00 24.34ATOM 2771 O HOH W 150 −1.333 15.279 37.020 1.00 28.81 ATOM 2772 O HOH W151 18.429 15.610 21.408 1.00 22.50 ATOM 2773 O HOH W 152 13.471 −4.26412.528 1.00 19.38 ATOM 2774 O HOH W 153 18.621 −17.600 7.222 1.00 21.52ATOM 2775 O HOH W 154 19.181 −5.396 13.023 1.00 33.83 ATOM 2776 O HOH W155 −3.698 −11.419 33.622 1.00 22.32 ATOM 2777 O HOH W 156 24.773 −7.68726.828 1.00 25.23 ATOM 2778 O HOH W 157 11.338 6.981 10.450 1.00 25.98ATOM 2779 O HOH W 158 7.187 4.097 9.722 1.00 25.73 ATOM 2780 O HOH W 15910.571 18.276 18.940 1.00 26.56 ATOM 2781 O HOH W 160 29.444 8.13818.655 1.00 25.10 ATOM 2782 O HOH W 161 −4.733 −16.782 12.321 1.00 23.51ATOM 2783 O HOH W 162 24.194 7.218 40.602 1.00 28.88 ATOM 2784 O HOH W163 13.925 −7.040 −5.961 1.00 29.58 ATOM 2785 O HOH W 164 −8.456 17.42510.469 1.00 25.03 ATOM 2786 O HOH W 165 20.283 7.809 6.109 1.00 25.58ATOM 2787 O HOH W 166 11.226 1.360 14.389 1.00 28.28 ATOM 2788 O HOH W167 17.600 11.985 25.766 1.00 28.21 ATOM 2789 O HOH W 168 −1.369 0.3646.150 1.00 26.61 ATOM 2790 O HOH W 169 1.250 6.912 6.112 1.00 22.96 ATOM2791 O HOH W 170 13.982 16.820 19.827 1.00 26.70 ATOM 2792 O HOH W 1718.401 6.117 8.285 1.00 29.37 ATOM 2793 O HOH W 172 1.561 32.980 20.3151.00 25.71 ATOM 2794 O HOH W 173 8.687 −4.960 0.724 1.00 20.63 ATOM 2795O HOH W 174 16.762 −8.584 32.541 1.00 22.53 ATOM 2796 O HOH W 175 −8.92823.790 25.122 1.00 26.68 ATOM 2797 O HOH W 176 30.774 −10.692 12.7811.00 29.33 ATOM 2798 O HOH W 177 −4.491 −0.583 48.435 1.00 27.59 ATOM2799 O HOH W 178 −10.254 8.887 25.677 1.00 27.41 ATOM 2800 O HOH W 17912.487 −14.347 0.366 1.00 29.02 ATOM 2801 O HOH W 180 −2.194 −3.1935.572 1.00 37.26 ATOM 2802 O HOH W 181 21.240 −14.747 4.723 1.00 24.12ATOM 2803 O HOH W 182 25.238 15.872 21.083 1.00 33.15 ATOM 2804 O HOH W183 27.650 8.541 12.497 1.00 23.15 ATOM 2805 O HOH W 184 35.303 3.83726.688 1.00 23.28 ATOM 2806 O HOH W 185 −3.730 14.555 34.107 1.00 23.34ATOM 2807 O HOH W 186 −8.927 −4.660 10.381 1.00 28.70 ATOM 2808 O HOH W187 40.695 −1.179 15.166 1.00 31.35 ATOM 2809 O HOH W 188 −0.356 −22.61531.607 1.00 35.28 ATOM 2810 O HOH W 189 3.463 34.674 22.382 1.00 27.20ATOM 2811 O HOH W 190 8.911 2.196 11.376 1.00 19.30 ATOM 2812 O HOH W191 −2.598 −24.115 28.861 1.00 26.04 ATOM 2813 O HOH W 192 8.418 −15.51034.179 1.00 38.02 ATOM 2814 O HOH W 193 15.703 −17.633 −0.060 1.00 35.88ATOM 2815 O HOH W 194 32.518 0.997 3.614 1.00 34.25 ATOM 2816 O HOH W195 19.062 −16.798 10.198 1.00 27.69 ATOM 2817 O HOH W 196 13.216 8.97610.392 1.00 27.61 ATOM 2818 O HOH W 197 2.647 −0.086 12.019 1.00 23.91ATOM 2819 O HOH W 198 −1.276 −7.561 35.325 1.00 25.96 ATOM 2820 O HOH W199 4.267 −22.362 30.170 1.00 35.68 ATOM 2821 O HOH W 200 21.787 10.59530.558 1.00 32.19 ATOM 2822 O HOH W 201 21.638 20.389 14.210 1.00 43.09ATOM 2823 O HOH W 202 5.373 −10.297 38.927 1.00 36.29 ATOM 2824 O HOH W203 29.035 −9.588 1.139 1.00 25.61 ATOM 2825 O HOH W 204 0.403 −17.62911.462 1.00 25.52 ATOM 2826 O HOH W 205 15.896 −2.824 23.429 1.00 9.81ATOM 2827 O HOH W 206 13.783 −1.283 21.923 1.00 12.03 ATOM 2828 O HOH W207 16.854 −0.738 21.328 1.00 11.76 ATOM 2829 O HOH W 208 14.946 −0.46519.263 1.00 10.55 ATOM 2830 O HOH W 209 −5.566 −9.500 29.835 1.00 34.12ATOM 2831 O HOH W 210 11.435 14.251 33.693 1.00 48.96 ATOM 2832 O HOH W211 3.944 31.281 18.816 1.00 43.83 ATOM 2833 O HOH W 212 21.511 8.20140.401 1.00 42.14 ATOM 2834 O HOH W 213 44.825 1.178 19.793 1.00 52.54ATOM 2835 O HOH W 214 9.397 20.244 23.958 1.00 30.91 ATOM 2836 O HOH W215 18.636 −1.182 15.865 1.00 23.82 ATOM 2837 O HOH W 216 18.955 −2.69317.957 1.00 28.82 ATOM 2838 O HOH W 217 26.248 −9.541 27.965 1.00 25.10ATOM 2839 O HOH W 218 24.703 −9.867 30.146 1.00 25.52 ATOM 2840 O HOH W219 22.600 −9.260 25.832 1.00 26.71 ATOM 2841 O HOH W 220 1.825 10.05439.457 1.00 25.12 ATOM 2842 O HOH W 221 3.585 4.590 45.058 1.00 28.59ATOM 2843 O HOH W 222 3.777 −6.424 30.447 1.00 24.42 TER 2844 HOH W 222ATOM 2845 ZN ZN B 864 13.210 0.069 20.406 1.00 15.15 ATOM 2846 MG MG B865 15.487 −0.725 23.006 1.00 8.84 TER 2847 MG B 865 END

[0217] TABLE 5 Atomic coordinates for PDE5* complex with UK-088,800 AtomNumber, Atom Type, Residue Type, Residue Number Cartesian Coordinates X,Y, Z, Atom Occupancy (O), Temperature Factor (B) and Atom Type X Y Z O BATOM 1 CB GLU A 536 9.887 25.182 24.787 1.00 33.98 ATOM 2 CG GLU A 53611.305 25.697 24.635 1.00 42.32 ATOM 3 CD GLU A 536 11.492 27.074 25.2451.00 47.12 ATOM 4 OE1 GLU A 536 11.290 27.223 26.470 1.00 54.45 ATOM 5OE2 GLU A 536 11.842 28.012 24.499 1.00 51.15 ATOM 6 C GLU A 536 7.94225.044 26.327 1.00 37.22 ATOM 7 O GLU A 536 7.222 24.272 25.690 1.0036.76 ATOM 8 N GLU A 536 9.991 23.667 26.752 1.00 36.93 ATOM 9 CA GLU A536 9.456 24.961 26.239 1.00 37.47 ATOM 10 N THR A 537 7.463 25.99027.125 1.00 37.34 ATOM 11 CA THR A 537 6.035 26.189 27.289 1.00 36.78ATOM 12 CB THR A 537 5.750 27.235 28.387 1.00 43.61 ATOM 13 OG1 THR A537 6.425 28.457 28.069 1.00 45.23 ATOM 14 CG2 THR A 537 6.241 26.73129.739 1.00 34.90 ATOM 15 C THR A 537 5.452 26.660 25.957 1.00 35.15ATOM 16 O THR A 537 4.239 26.661 25.764 1.00 34.30 ATOM 17 N ARG A 5386.336 27.046 25.040 1.00 32.72 ATOM 18 CA ARG A 538 5.943 27.514 23.7121.00 31.35 ATOM 19 CB ARG A 538 7.143 28.133 23.002 1.00 33.78 ATOM 20CG ARG A 538 6.910 28.452 21.531 1.00 42.77 ATOM 21 CD ARG A 538 6.04129.690 21.340 1.00 51.85 ATOM 22 NE ARG A 538 4.638 29.475 21.687 1.0050.21 ATOM 23 CZ ARG A 538 3.715 30.433 21.672 1.00 49.57 ATOM 24 NH1ARG A 538 4.047 31.673 21.330 1.00 48.08 ATOM 25 NH2 ARG A 538 2.45830.154 21.992 1.00 49.14 ATOM 26 C ARG A 538 5.405 26.369 22.861 1.0030.33 ATOM 27 O ARG A 538 4.381 26.501 22.187 1.00 28.72 ATOM 28 N GLU A539 6.120 25.250 22.876 1.00 28.94 ATOM 29 CA GLU A 539 5.709 24.08022.115 1.00 25.47 ATOM 30 CB GLU A 539 6.807 23.024 22.141 1.00 30.35ATOM 31 CG GLU A 539 8.055 23.426 21.391 1.00 31.75 ATOM 32 CD GLU A 5399.188 22.463 21.628 1.00 31.48 ATOM 33 OE1 GLU A 539 9.689 22.410 22.7711.00 46.55 ATOM 34 OE2 GLU A 539 9.575 21.754 20.676 1.00 57.06 ATOM 35C GLU A 539 4.437 23.511 22.718 1.00 23.49 ATOM 36 O GLU A 539 3.59922.952 22.011 1.00 21.01 ATOM 37 N LEU A 540 4.299 23.653 24.032 1.0022.37 ATOM 38 CA LEU A 540 3.114 23.159 24.713 1.00 22.10 ATOM 39 CB LEUA 540 3.302 23.223 26.231 1.00 19.44 ATOM 40 CG LEU A 540 2.098 22.76327.059 1.00 22.04 ATOM 41 CD1 LEU A 540 1.686 21.365 26.627 1.00 19.81ATOM 42 CD2 LEU A 540 2.441 22.783 28.539 1.00 38.12 ATOM 43 C LEU A 5401.907 23.995 24.300 1.00 21.23 ATOM 44 O LEU A 540 0.844 23.461 23.9901.00 19.37 ATOM 45 N GLN A 541 2.074 25.313 24.283 1.00 20.36 ATOM 46 CAGLN A 541 0.972 26.185 23.905 1.00 18.42 ATOM 47 CB GLN A 541 1.41027.651 23.966 1.00 20.67 ATOM 48 CG GLN A 541 1.873 28.081 25.350 1.0024.12 ATOM 49 CD GLN A 541 2.356 29.519 25.401 1.00 24.37 ATOM 50 OE1GLN A 541 3.047 29.986 24.497 1.00 17.86 ATOM 51 NE2 GLN A 541 2.00830.223 26.474 1.00 20.12 ATOM 52 C GLN A 541 0.477 25.833 22.505 1.0017.74 ATOM 53 O GLN A 541 −0.726 25.799 22.254 1.00 19.08 ATOM 54 N SERA 542 1.404 25.552 21.596 1.00 15.82 ATOM 55 CA SER A 542 1.026 25.20720.231 1.00 18.42 ATOM 56 CB SER A 542 2.263 25.179 19.329 1.00 20.91ATOM 57 OG SER A 542 2.857 26.463 19.251 1.00 37.22 ATOM 58 C SER A 5420.320 23.858 20.174 1.00 16.82 ATOM 59 O SER A 542 −0.710 23.709 19.5201.00 17.71 ATOM 60 N LEU A 543 0.875 22.874 20.872 1.00 17.64 ATOM 61 CALEU A 543 0.297 21.538 20.878 1.00 17.88 ATOM 62 CB LEU A 543 1.26920.550 21.531 1.00 13.54 ATOM 63 CG LEU A 543 0.762 19.113 21.695 1.0017.02 ATOM 64 CD1 LEU A 543 0.501 18.504 20.329 1.00 14.15 ATOM 65 CD2LEU A 543 1.789 18.284 22.465 1.00 10.59 ATOM 66 C LEU A 543 −1.04921.468 21.592 1.00 18.33 ATOM 67 O LEU A 543 −2.013 20.914 21.064 1.0019.18 ATOM 68 N ALA A 544 −1.112 22.038 22.790 1.00 18.60 ATOM 69 CA ALAA 544 −2.332 22.003 23.588 1.00 19.09 ATOM 70 CB ALA A 544 −2.053 22.57324.972 1.00 17.83 ATOM 71 C ALA A 544 −3.527 22.717 22.967 1.00 21.56ATOM 72 O ALA A 544 −4.667 22.306 23.165 1.00 23.51 ATOM 73 N ALA A 545−3.269 23.782 22.217 1.00 23.98 ATOM 74 CA ALA A 545 −4.348 24.54721.599 1.00 24.34 ATOM 75 CB ALA A 545 −3.861 25.952 21.274 1.00 26.53ATOM 76 C ALA A 545 −4.901 23.891 20.341 1.00 25.76 ATOM 77 O ALA A 545−6.065 24.079 19.992 1.00 28.16 ATOM 78 N ALA A 546 −4.059 23.115 19.6681.00 24.74 ATOM 79 CA ALA A 546 −4.441 22.443 18.430 1.00 24.22 ATOM 80CB ALA A 546 −3.239 21.701 17.861 1.00 22.00 ATOM 81 C ALA A 546 −5.62121.485 18.529 1.00 21.89 ATOM 82 O ALA A 546 −5.803 20.791 19.529 1.0023.27 ATOM 83 N VAL A 547 −6.433 21.464 17.478 1.00 21.72 ATOM 84 CA VALA 547 −7.560 20.548 17.418 1.00 21.65 ATOM 85 CB VAL A 547 −8.660 21.04516.454 1.00 23.33 ATOM 86 CG1 VAL A 547 −9.754 19.993 16.326 1.00 25.11ATOM 87 CG2 VAL A 547 −9.250 22.355 16.965 1.00 23.58 ATOM 88 C VAL A547 −6.925 19.284 16.850 1.00 22.28 ATOM 89 O VAL A 547 −6.280 19.32915.805 1.00 24.96 ATOM 90 N VAL A 548 −7.090 18.165 17.542 1.00 21.82ATOM 91 CA VAL A 548 −6.498 16.909 17.098 1.00 19.25 ATOM 92 CB VAL A548 −6.387 15.925 18.278 1.00 19.56 ATOM 93 CG1 VAL A 548 −5.669 14.65917.840 1.00 23.78 ATOM 94 CG2 VAL A 548 −5.656 16.593 19.438 1.00 24.95ATOM 95 C VAL A 548 −7.284 16.241 15.975 1.00 17.26 ATOM 96 O VAL A 548−8.453 15.904 16.146 1.00 19.24 ATOM 97 N PRO A 549 −6.646 16.038 14.8081.00 17.33 ATOM 98 CD PRO A 549 −5.293 16.478 14.431 1.00 18.64 ATOM 99CA PRO A 549 −7.315 15.401 13.670 1.00 19.43 ATOM 100 CB PRO A 549−6.245 15.425 12.575 1.00 17.30 ATOM 101 CG PRO A 549 −5.420 16.61512.931 1.00 23.24 ATOM 102 C PRO A 549 −7.742 13.982 14.023 1.00 20.23ATOM 103 O PRO A 549 −7.259 13.402 15.001 1.00 16.82 ATOM 104 N SER A550 −8.645 13.431 13.220 1.00 17.57 ATOM 105 CA SER A 550 −9.153 12.08113.432 1.00 20.68 ATOM 106 CB SER A 550 −10.343 11.822 12.512 1.00 17.19ATOM 107 OG SER A 550 −9.934 11.861 11.153 1.00 18.60 ATOM 108 C SER A550 −8.075 11.055 13.127 1.00 17.34 ATOM 109 O SER A 550 −7.096 11.35712.443 1.00 16.71 ATOM 110 N ALA A 551 −8.257 9.841 13.637 1.00 18.46ATOM 111 CA ALA A 551 −7.304 8.769 13.380 1.00 19.34 ATOM 112 CB ALA A551 −7.706 7.507 14.143 1.00 17.06 ATOM 113 C ALA A 551 −7.322 8.50211.879 1.00 18.62 ATOM 114 O ALA A 551 −6.284 8.262 11.261 1.00 20.73ATOM 115 N GLN A 552 −8.518 8.554 11.300 1.00 19.78 ATOM 116 CA GLN A552 −8.700 8.327 9.869 1.00 21.36 ATOM 117 CB GLN A 552 −10.175 8.5289.502 1.00 23.40 ATOM 118 CG GLN A 552 −10.541 8.181 8.067 1.00 31.79ATOM 119 CD GLN A 552 −12.026 8.358 7.797 1.00 35.80 ATOM 120 OE1 GLN A552 −12.864 7.675 8.390 1.00 46.36 ATOM 121 NE2 GLN A 552 −12.358 9.2836.902 1.00 49.03 ATOM 122 C GLN A 552 −7.820 9.301 9.086 1.00 21.35 ATOM123 O GLN A 552 −7.040 8.897 8.219 1.00 21.48 ATOM 124 N THR A 553−7.938 10.584 9.408 1.00 19.75 ATOM 125 CA THR A 553 −7.151 11.612 8.7391.00 19.52 ATOM 126 CB THR A 553 −7.501 13.017 9.268 1.00 18.18 ATOM 127OG1 THR A 553 −8.871 13.318 8.971 1.00 19.96 ATOM 128 CG2 THR A 553−6.597 14.066 8.627 1.00 18.92 ATOM 129 C THR A 553 −5.654 11.396 8.9261.00 20.00 ATOM 130 O THR A 553 −4.875 11.523 7.980 1.00 19.53 ATOM 131N LEU A 554 −5.260 11.062 10.150 1.00 19.10 ATOM 132 CA LEU A 554 −3.85510.853 10.474 1.00 20.03 ATOM 133 CB LEU A 554 −3.650 10.974 11.987 1.0017.91 ATOM 134 CG LEU A 554 −4.091 12.323 12.571 1.00 18.40 ATOM 135 CD1LEU A 554 −3.972 12.316 14.082 1.00 16.11 ATOM 136 CD2 LEU A 554 −3.23713.436 11.977 1.00 23.68 ATOM 137 C LEU A 554 −3.303 9.521 9.970 1.0019.88 ATOM 138 O LEU A 554 −2.093 9.304 9.994 1.00 19.74 ATOM 139 N LYSA 555 −4.198 8.637 9.533 1.00 17.37 ATOM 140 CA LYS A 555 −3.833 7.3278.997 1.00 19.69 ATOM 141 CB LYS A 555 −3.032 7.523 7.708 1.00 26.45ATOM 142 CG LYS A 555 −3.740 8.429 6.708 1.00 33.54 ATOM 143 CD LYS A555 −2.829 8.837 5.565 1.00 36.95 ATOM 144 CE LYS A 555 −3.542 9.8034.633 1.00 36.53 ATOM 145 NZ LYS A 555 −2.645 10.308 3.562 1.00 43.43ATOM 146 C LYS A 555 −3.043 6.454 9.976 1.00 19.45 ATOM 147 O LYS A 555−2.294 5.569 9.565 1.00 18.29 ATOM 148 N ILE A 556 −3.227 6.688 11.2711.00 17.06 ATOM 149 CA ILE A 556 −2.501 5.917 12.273 1.00 16.83 ATOM 150CB ILE A 556 −2.475 6.638 13.641 1.00 13.95 ATOM 151 CG2 ILE A 556−1.565 7.856 13.569 1.00 16.87 ATOM 152 CG1 ILE A 556 −3.897 7.01714.062 1.00 14.93 ATOM 153 CD1 ILE A 556 −3.981 7.598 15.460 1.00 19.73ATOM 154 C ILE A 556 −3.019 4.496 12.489 1.00 14.60 ATOM 155 O ILE A 556−2.443 3.745 13.271 1.00 12.74 ATOM 156 N THR A 557 −4.099 4.125 11.8061.00 14.27 ATOM 157 CA THR A 557 −4.653 2.776 11.938 1.00 15.05 ATOM 158CB THR A 557 −6.187 2.772 11.699 1.00 21.22 ATOM 159 OG1 THR A 557−6.813 3.726 12.567 1.00 20.77 ATOM 160 CG2 THR A 557 −6.773 1.39811.982 1.00 21.26 ATOM 161 C THR A 557 −3.991 1.855 10.907 1.00 14.39ATOM 162 O THR A 557 −4.131 0.631 10.955 1.00 16.89 ATOM 163 N ASP A 558−3.257 2.456 9.979 1.00 14.56 ATOM 164 CA ASP A 558 −2.593 1.702 8.9231.00 14.77 ATOM 165 CB ASP A 558 −2.374 2.613 7.713 1.00 20.77 ATOM 166CG ASP A 558 −3.648 3.312 7.274 1.00 30.09 ATOM 167 OD1 ASP A 558 −4.6572.616 7.031 1.00 38.75 ATOM 168 OD2 ASP A 558 −3.642 4.555 7.173 1.0046.69 ATOM 169 C ASP A 558 −1.258 1.086 9.351 1.00 14.68 ATOM 170 O ASPA 558 −0.365 1.787 9.829 1.00 13.87 ATOM 171 N PHE A 559 −1.124 −0.2279.175 1.00 13.82 ATOM 172 CA PHE A 559 0.119 −0.916 9.526 1.00 13.07ATOM 173 CB PHE A 559 0.000 −2.427 9.283 1.00 14.41 ATOM 174 CG PHE A559 −0.732 −3.175 10.366 1.00 18.21 ATOM 175 CD1 PHE A 559 −0.289 −3.13411.680 1.00 14.30 ATOM 176 CD2 PHE A 559 −1.836 −3.960 10.060 1.00 16.61ATOM 177 CE1 PHE A 559 −0.931 −3.866 12.668 1.00 15.41 ATOM 178 CE2 PHEA 559 −2.482 −4.692 11.043 1.00 15.41 ATOM 179 CZ PHE A 559 −2.031−4.647 12.344 1.00 12.10 ATOM 180 C PHE A 559 1.277 −0.386 8.680 1.0011.71 ATOM 181 O PHE A 559 2.431 −0.411 9.109 1.00 12.25 ATOM 182 N SERA 560 0.965 0.079 7.473 1.00 13.82 ATOM 183 CA SER A 560 1.979 0.5976.555 1.00 13.86 ATOM 184 CB SER A 560 1.538 0.384 5.106 1.00 19.52 ATOM185 OG SER A 560 1.411 −0.996 4.816 1.00 19.35 ATOM 186 C SER A 5602.294 2.071 6.770 1.00 12.88 ATOM 187 O SER A 560 2.959 2.698 5.945 1.0014.29 ATOM 188 N PHE A 561 1.815 2.608 7.886 1.00 12.82 ATOM 189 CA PHEA 561 2.021 4.009 8.261 1.00 13.63 ATOM 190 CB PHE A 561 1.567 4.2079.713 1.00 14.59 ATOM 191 CG PHE A 561 1.835 5.583 10.258 1.00 12.08ATOM 192 CD1 PHE A 561 0.956 6.625 10.014 1.00 17.74 ATOM 193 CD2 PHE A561 2.967 5.829 11.022 1.00 10.31 ATOM 194 CE1 PHE A 561 1.199 7.89110.524 1.00 21.75 ATOM 195 CE2 PHE A 561 3.220 7.093 11.537 1.00 13.27ATOM 196 CZ PHE A 561 2.333 8.126 11.287 1.00 18.85 ATOM 197 C PHE A 5613.466 4.498 8.125 1.00 14.38 ATOM 198 O PHE A 561 4.413 3.791 8.485 1.0011.10 ATOM 199 N SER A 562 3.625 5.716 7.607 1.00 14.38 ATOM 200 CA SERA 562 4.939 6.334 7.453 1.00 13.72 ATOM 201 CB SER A 562 5.283 6.5205.972 1.00 15.96 ATOM 202 OG SER A 562 6.542 7.159 5.835 1.00 23.25 ATOM203 C SER A 562 4.940 7.695 8.159 1.00 12.53 ATOM 204 O SER A 562 4.0098.490 8.014 1.00 12.55 ATOM 205 N ASP A 563 5.992 7.965 8.922 1.00 13.45ATOM 206 CA ASP A 563 6.094 9.223 9.661 1.00 15.79 ATOM 207 CB ASP A 5636.662 8.953 11.050 1.00 13.73 ATOM 208 CG ASP A 563 8.166 8.765 11.0221.00 15.49 ATOM 209 OD1 ASP A 563 8.895 9.680 11.465 1.00 18.81 ATOM 210OD2 ASP A 563 8.625 7.712 10.537 1.00 16.12 ATOM 211 C ASP A 563 7.00910.232 8.974 1.00 16.63 ATOM 212 O ASP A 563 7.112 11.383 9.404 1.0017.82 ATOM 213 N PHE A 564 7.673 9.796 7.911 1.00 16.51 ATOM 214 CA PHEA 564 8.633 10.635 7.205 1.00 18.23 ATOM 215 CB PHE A 564 9.207 9.8716.011 1.00 15.87 ATOM 216 CG PHE A 564 10.446 10.494 5.438 1.00 26.61ATOM 217 CD1 PHE A 564 11.599 10.592 6.201 1.00 20.64 ATOM 218 CD2 PHE A564 10.458 10.991 4.144 1.00 27.32 ATOM 219 CE1 PHE A 564 12.742 11.1745.685 1.00 30.38 ATOM 220 CE2 PHE A 564 11.599 11.574 3.622 1.00 33.45ATOM 221 CZ PHE A 564 12.742 11.665 4.394 1.00 33.80 ATOM 222 C PHE A564 8.157 12.010 6.740 1.00 18.52 ATOM 223 O PHE A 564 8.942 12.9596.728 1.00 19.54 ATOM 224 N GLU A 565 6.885 12.122 6.369 1.00 16.14 ATOM225 CA GLU A 565 6.340 13.391 5.890 1.00 19.03 ATOM 226 CB GLU A 5655.277 13.142 4.813 1.00 18.54 ATOM 227 CG GLU A 565 5.708 12.238 3.6681.00 33.46 ATOM 228 CD GLU A 565 6.004 10.818 4.117 1.00 40.92 ATOM 229OE1 GLU A 565 5.205 10.258 4.899 1.00 41.02 ATOM 230 OE2 GLU A 565 7.03210.259 3.680 1.00 50.71 ATOM 231 C GLU A 565 5.710 14.229 7.002 1.0019.43 ATOM 232 O GLU A 565 5.158 15.301 6.740 1.00 20.33 ATOM 233 N LEUA 566 5.786 13.746 8.238 1.00 13.91 ATOM 234 CA LEU A 566 5.193 14.4639.362 1.00 15.26 ATOM 235 CB LEU A 566 4.515 13.482 10.321 1.00 15.63ATOM 236 CG LEU A 566 3.329 12.669 9.799 1.00 24.63 ATOM 237 CD1 LEU A566 2.864 11.698 10.881 1.00 23.72 ATOM 238 CD2 LEU A 566 2.199 13.6079.399 1.00 33.15 ATOM 239 C LEU A 566 6.187 15.306 10.147 1.00 14.43ATOM 240 O LEU A 566 7.358 14.960 10.265 1.00 17.81 ATOM 241 N SER A 5675.699 16.419 10.685 1.00 14.78 ATOM 242 CA SER A 567 6.517 17.317 11.4861.00 14.98 ATOM 243 CB SER A 567 5.928 18.727 11.467 1.00 21.89 ATOM 244OG SER A 567 4.679 18.752 12.144 1.00 17.63 ATOM 245 C SER A 567 6.49216.797 12.922 1.00 13.89 ATOM 246 O SER A 567 5.654 15.963 13.268 1.0013.82 ATOM 247 N ASP A 568 7.403 17.289 13.753 1.00 15.43 ATOM 248 CAASP A 568 7.428 16.869 15.149 1.00 15.57 ATOM 249 CB ASP A 568 8.53617.603 15.904 1.00 19.60 ATOM 250 CG ASP A 568 9.888 16.947 15.727 1.0016.75 ATOM 251 OD1 ASP A 568 9.989 16.021 14.899 1.00 19.05 ATOM 252 OD2ASP A 568 10.848 17.355 16.415 1.00 23.47 ATOM 253 C ASP A 568 6.07617.145 15.805 1.00 16.52 ATOM 254 O ASP A 568 5.559 16.313 16.556 1.0015.97 ATOM 255 N LEU A 569 5.505 18.311 15.516 1.00 15.09 ATOM 256 CALEU A 569 4.213 18.683 16.076 1.00 15.08 ATOM 257 CB LEU A 569 3.81520.093 15.620 1.00 16.05 ATOM 258 CG LEU A 569 2.385 20.516 15.974 1.0023.47 ATOM 259 CD1 LEU A 569 2.203 20.527 17.489 1.00 21.65 ATOM 260 CD2LEU A 569 2.103 21.896 15.398 1.00 27.54 ATOM 261 C LEU A 569 3.13617.694 15.647 1.00 12.90 ATOM 262 O LEU A 569 2.279 17.308 16.441 1.0016.26 ATOM 263 N GLU A 570 3.184 17.281 14.386 1.00 13.40 ATOM 264 CAGLU A 570 2.202 16.340 13.869 1.00 14.08 ATOM 265 CB GLU A 570 2.35416.196 12.352 1.00 14.43 ATOM 266 CG GLU A 570 1.885 17.432 11.579 1.0020.85 ATOM 267 CD GLU A 570 2.062 17.291 10.081 1.00 23.63 ATOM 268 OE1GLU A 570 3.218 17.158 9.632 1.00 21.68 ATOM 269 OE2 GLU A 570 1.04717.311 9.352 1.00 28.09 ATOM 270 C GLU A 570 2.309 14.978 14.547 1.0014.43 ATOM 271 O GLU A 570 1.293 14.319 14.780 1.00 15.20 ATOM 272 N THRA 571 3.529 14.551 14.866 1.00 12.67 ATOM 273 CA THR A 571 3.694 13.25915.538 1.00 12.83 ATOM 274 CB THR A 571 5.182 12.816 15.638 1.00 13.30ATOM 275 OG1 THR A 571 5.915 13.737 16.452 1.00 12.68 ATOM 276 CG2 THR A571 5.817 12.738 14.250 1.00 12.38 ATOM 277 C THR A 571 3.110 13.36016.945 1.00 11.29 ATOM 278 O THR A 571 2.589 12.381 17.483 1.00 12.14ATOM 279 N ALA A 572 3.202 14.548 17.538 1.00 12.42 ATOM 280 CA ALA A572 2.659 14.780 18.869 1.00 11.84 ATOM 281 CB ALA A 572 3.090 16.14219.388 1.00 12.18 ATOM 282 C ALA A 572 1.136 14.701 18.803 1.00 13.34ATOM 283 O ALA A 572 0.500 14.128 19.683 1.00 11.72 ATOM 284 N LEU A 5730.554 15.283 17.758 1.00 12.67 ATOM 285 CA LEU A 573 −0.894 15.24417.583 1.00 13.98 ATOM 286 CB LEU A 573 −1.307 16.104 16.384 1.00 14.33ATOM 287 CG LEU A 573 −1.135 17.619 16.544 1.00 14.55 ATOM 288 CD1 LEU A573 −1.445 18.310 15.224 1.00 21.57 ATOM 289 CD2 LEU A 573 −2.061 18.12517.647 1.00 20.27 ATOM 290 C LEU A 573 −1.338 13.795 17.366 1.00 15.26ATOM 291 O LEU A 573 −2.394 13.378 17.853 1.00 15.01 ATOM 292 N CYS A574 −0.534 13.030 16.632 1.00 13.44 ATOM 293 CA CYS A 574 −0.852 11.62516.385 1.00 13.06 ATOM 294 CB CYS A 574 0.187 10.974 15.470 1.00 12.27ATOM 295 SG CYS A 574 0.049 11.382 13.714 1.00 15.24 ATOM 296 C CYS A574 −0.873 10.864 17.703 1.00 12.15 ATOM 297 O CYS A 574 −1.710 9.99117.919 1.00 13.51 ATOM 298 N THR A 575 0.066 11.194 18.581 1.00 11.60ATOM 299 CA THR A 575 0.158 10.532 19.872 1.00 12.28 ATOM 300 CB THR A575 1.453 10.949 20.592 1.00 10.90 ATOM 301 OG1 THR A 575 2.575 10.57619.777 1.00 13.47 ATOM 302 CG2 THR A 575 1.565 10.264 21.944 1.00 10.06ATOM 303 C THR A 575 −1.068 10.841 20.726 1.00 11.74 ATOM 304 O THR A575 −1.613 9.952 21.379 1.00 10.78 ATOM 305 N ILE A 576 −1.514 12.09520.717 1.00 12.29 ATOM 306 CA ILE A 576 −2.700 12.453 21.484 1.00 11.92ATOM 307 CB ILE A 576 −3.046 13.945 21.354 1.00 11.38 ATOM 308 CG2 ILE A576 −4.371 14.222 22.053 1.00 12.83 ATOM 309 CG1 ILE A 576 −1.933 14.80221.965 1.00 17.73 ATOM 310 CD1 ILE A 576 −2.154 16.292 21.798 1.00 13.34ATOM 311 C ILE A 576 −3.880 11.636 20.960 1.00 12.34 ATOM 312 O ILE A576 −4.674 11.103 21.737 1.00 13.64 ATOM 313 N ARG A 577 −3.985 11.53219.638 1.00 13.14 ATOM 314 CA ARG A 577 −5.071 10.772 19.032 1.00 13.22ATOM 315 CB ARG A 577 −5.029 10.888 17.503 1.00 12.21 ATOM 316 CG ARG A577 −6.113 10.084 16.795 1.00 12.42 ATOM 317 CD ARG A 577 −7.492 10.38317.365 1.00 10.79 ATOM 318 NE ARG A 577 −7.912 11.757 17.111 1.00 18.46ATOM 319 CZ ARG A 577 −9.015 12.304 17.612 1.00 16.47 ATOM 320 NH1 ARG A577 −9.319 13.564 17.325 1.00 24.31 ATOM 321 NH2 ARG A 577 −9.809 11.59618.405 1.00 18.21 ATOM 322 C ARG A 577 −5.029 9.304 19.455 1.00 12.45ATOM 323 O ARG A 577 −6.069 8.675 19.625 1.00 11.98 ATOM 324 N MET A 578−3.831 8.756 19.630 1.00 10.43 ATOM 325 CA MET A 578 −3.716 7.367 20.0581.00 11.28 ATOM 326 CB MET A 578 −2.245 6.934 20.090 1.00 11.91 ATOM 327CG MET A 578 −1.605 6.808 18.716 1.00 12.93 ATOM 328 SD MET A 578 0.1346.324 18.830 1.00 16.07 ATOM 329 CE MET A 578 0.781 7.021 17.300 1.0019.76 ATOM 330 C MET A 578 −4.332 7.191 21.445 1.00 12.18 ATOM 331 O META 578 −5.103 6.260 21.675 1.00 11.26 ATOM 332 N PHE A 579 −3.982 8.08022.372 1.00 11.60 ATOM 333 CA PHE A 579 −4.521 8.004 23.725 1.00 11.60ATOM 334 CB PHE A 579 −3.921 9.097 24.619 1.00 12.17 ATOM 335 CG PHE A579 −2.584 8.748 25.201 1.00 9.68 ATOM 336 CD1 PHE A 579 −1.415 9.02324.510 1.00 13.42 ATOM 337 CD2 PHE A 579 −2.497 8.148 26.450 1.00 12.49ATOM 338 CE1 PHE A 579 −0.178 8.709 25.054 1.00 10.87 ATOM 339 CE2 PHE A579 −1.264 7.829 27.000 1.00 13.01 ATOM 340 CZ PHE A 579 −0.103 8.11326.301 1.00 12.83 ATOM 341 C PHE A 579 −6.040 8.170 23.708 1.00 12.84ATOM 342 O PHE A 579 −6.765 7.429 24.367 1.00 12.73 ATOM 343 N THR A 580−6.504 9.151 22.943 1.00 15.04 ATOM 344 CA THR A 580 −7.926 9.459 22.8391.00 14.30 ATOM 345 CB THR A 580 −8.145 10.702 21.967 1.00 10.78 ATOM346 OG1 THR A 580 −7.344 11.780 22.469 1.00 18.08 ATOM 347 CG2 THR A 580−9.610 11.115 21.987 1.00 13.16 ATOM 348 C THR A 580 −8.772 8.327 22.2731.00 14.34 ATOM 349 O THR A 580 −9.774 7.936 22.871 1.00 14.67 ATOM 350N ASP A 581 −8.367 7.806 21.119 1.00 15.75 ATOM 351 CA ASP A 581 −9.1066.731 20.466 1.00 14.61 ATOM 352 CB ASP A 581 −8.724 6.668 18.990 1.0016.27 ATOM 353 CG ASP A 581 −9.398 7.757 18.181 1.00 20.38 ATOM 354 OD1ASP A 581 −9.762 8.797 18.776 1.00 15.70 ATOM 355 OD2 ASP A 581 −9.5607.580 16.958 1.00 17.57 ATOM 356 C ASP A 581 −8.970 5.365 21.123 1.0015.19 ATOM 357 O ASP A 581 −9.627 4.402 20.719 1.00 14.62 ATOM 358 N LEUA 582 −8.110 5.275 22.130 1.00 13.55 ATOM 359 CA LEU A 582 −7.957 4.03222.867 1.00 14.36 ATOM 360 CB LEU A 582 −6.484 3.739 23.156 1.00 16.24ATOM 361 CG LEU A 582 −5.770 3.024 22.006 1.00 14.56 ATOM 362 CD1 LEU A582 −4.272 2.968 22.250 1.00 12.82 ATOM 363 CD2 LEU A 582 −6.351 1.62521.865 1.00 12.05 ATOM 364 C LEU A 582 −8.739 4.189 24.168 1.00 17.31ATOM 365 O LEU A 582 −8.617 3.378 25.081 1.00 17.82 ATOM 366 N ASN A 583−9.533 5.255 24.246 1.00 17.93 ATOM 367 CA ASN A 583 −10.361 5.50025.420 1.00 21.01 ATOM 368 CB ASN A 583 −11.405 4.377 25.525 1.00 22.07ATOM 369 CG ASN A 583 −12.368 4.564 26.682 1.00 34.95 ATOM 370 OD1 ASN A583 −12.921 5.645 26.879 1.00 34.93 ATOM 371 ND2 ASN A 583 −12.589 3.49627.444 1.00 39.94 ATOM 372 C ASN A 583 −9.516 5.575 26.693 1.00 23.16ATOM 373 O ASN A 583 −9.866 4.978 27.713 1.00 27.41 ATOM 374 N LEU A 584−8.406 6.313 26.634 1.00 18.24 ATOM 375 CA LEU A 584 −7.517 6.446 27.7911.00 18.39 ATOM 376 CB LEU A 584 −6.060 6.188 27.379 1.00 13.74 ATOM 377CG LEU A 584 −5.713 4.823 26.778 1.00 13.61 ATOM 378 CD1 LEU A 584−4.226 4.789 26.412 1.00 16.18 ATOM 379 CD2 LEU A 584 −6.050 3.72627.769 1.00 15.78 ATOM 380 C LEU A 584 −7.591 7.807 28.486 1.00 18.85ATOM 381 O LEU A 584 −7.377 7.904 29.695 1.00 18.54 ATOM 382 N VAL A 585−7.890 8.853 27.721 1.00 18.53 ATOM 383 CA VAL A 585 −7.956 10.21128.258 1.00 20.90 ATOM 384 CB VAL A 585 −8.157 11.234 27.123 1.00 25.63ATOM 385 CG1 VAL A 585 −8.083 12.648 27.672 1.00 26.57 ATOM 386 CG2 VALA 585 −7.102 11.024 26.054 1.00 26.78 ATOM 387 C VAL A 585 −9.049 10.41629.307 1.00 21.72 ATOM 388 O VAL A 585 −8.771 10.839 30.429 1.00 21.94ATOM 389 N GLN A 586 −10.291 10.118 28.945 1.00 22.79 ATOM 390 CA GLN A586 −11.394 10.290 29.881 1.00 25.11 ATOM 391 CB GLN A 586 −12.72810.306 29.131 1.00 34.29 ATOM 392 CG GLN A 586 −13.719 11.317 29.6781.00 39.65 ATOM 393 CD GLN A 586 −13.155 12.725 29.663 1.00 50.17 ATOM394 OE1 GLN A 586 −12.715 13.218 28.622 1.00 52.20 ATOM 395 NE2 GLN A586 −13.160 13.380 30.820 1.00 48.68 ATOM 396 C GLN A 586 −11.402 9.17230.914 1.00 22.36 ATOM 397 O GLN A 586 −11.587 9.413 32.108 1.00 23.81ATOM 398 N ASN A 587 −11.195 7.948 30.441 1.00 22.47 ATOM 399 CA ASN A587 −11.181 6.769 31.298 1.00 19.07 ATOM 400 CB ASN A 587 −10.651 5.56530.507 1.00 21.06 ATOM 401 CG ASN A 587 −10.944 4.236 31.179 1.00 29.14ATOM 402 OD1 ASN A 587 −11.098 4.157 32.397 1.00 21.26 ATOM 403 ND2 ASNA 587 −11.002 3.174 30.382 1.00 33.44 ATOM 404 C ASN A 587 −10.319 6.98132.542 1.00 20.86 ATOM 405 O ASN A 587 −10.727 6.646 33.656 1.00 19.43ATOM 406 N PHE A 588 −9.134 7.553 32.357 1.00 18.57 ATOM 407 CA PHE A588 −8.227 7.753 33.480 1.00 18.65 ATOM 408 CB PHE A 588 −6.880 7.10933.145 1.00 13.88 ATOM 409 CG PHE A 588 −6.976 5.624 32.948 1.00 14.75ATOM 410 CD1 PHE A 588 −7.272 4.791 34.022 1.00 13.58 ATOM 411 CD2 PHE A588 −6.860 5.065 31.686 1.00 12.05 ATOM 412 CE1 PHE A 588 −7.456 3.43133.837 1.00 13.16 ATOM 413 CE2 PHE A 588 −7.044 3.704 31.496 1.00 10.45ATOM 414 CZ PHE A 588 −7.344 2.888 32.576 1.00 16.21 ATOM 415 C PHE A588 −8.063 9.190 33.966 1.00 20.57 ATOM 416 O PHE A 588 −7.072 9.53834.611 1.00 18.90 ATOM 417 N GLN A 589 −9.052 10.020 33.662 1.00 21.41ATOM 418 CA GLN A 589 −9.057 11.410 34.110 1.00 23.36 ATOM 419 CB GLN A589 −9.213 11.449 35.634 1.00 28.73 ATOM 420 CG GLN A 589 −10.311 10.55136.194 1.00 40.43 ATOM 421 CD GLN A 589 −11.701 11.003 35.797 1.00 42.17ATOM 422 OE1 GLN A 589 −12.058 12.167 35.971 1.00 38.12 ATOM 423 NE2 GLNA 589 −12.498 10.080 35.270 1.00 47.35 ATOM 424 C GLN A 589 −7.80512.201 33.725 1.00 20.90 ATOM 425 O GLN A 589 −7.282 12.972 34.531 1.0021.16 ATOM 426 N MET A 590 −7.321 12.019 32.502 1.00 22.12 ATOM 427 CAMET A 590 −6.133 12.745 32.069 1.00 21.73 ATOM 428 CB MET A 590 −5.46312.035 30.893 1.00 22.93 ATOM 429 CG MET A 590 −4.751 10.752 31.257 1.0024.06 ATOM 430 SD MET A 590 −3.865 10.087 29.838 1.00 19.72 ATOM 431 CEMET A 590 −3.631 8.404 30.357 1.00 17.35 ATOM 432 C MET A 590 −6.45514.172 31.654 1.00 22.68 ATOM 433 O MET A 590 −7.295 14.398 30.784 1.0023.69 ATOM 434 N LYS A 591 −5.792 15.138 32.278 1.00 20.35 ATOM 435 CALYS A 591 −6.013 16.530 31.919 1.00 20.85 ATOM 436 CB LYS A 591 −5.55417.460 33.045 1.00 22.95 ATOM 437 CG LYS A 591 −6.472 17.422 34.262 1.0028.61 ATOM 438 CD LYS A 591 −6.065 18.438 35.315 1.00 37.59 ATOM 439 CELYS A 591 −7.106 18.527 36.423 1.00 42.92 ATOM 440 NZ LYS A 591 −8.41719.026 35.915 1.00 51.43 ATOM 441 C LYS A 591 −5.235 16.800 30.636 1.0020.72 ATOM 442 O LYS A 591 −4.048 16.486 30.537 1.00 21.29 ATOM 443 NHIS A 592 −5.920 17.375 29.654 1.00 20.84 ATOM 444 CA HIS A 592 −5.33317.670 28.351 1.00 21.11 ATOM 445 CB HIS A 592 −6.273 18.577 27.553 1.0021.39 ATOM 446 CG HIS A 592 −5.884 18.737 26.125 1.00 18.05 ATOM 447 CD2HIS A 592 −5.427 19.798 25.424 1.00 24.75 ATOM 448 ND1 HIS A 592 −5.92617.685 25.213 1.00 22.74 ATOM 449 CE1 HIS A 592 −5.518 18.102 24.0441.00 29.20 ATOM 450 NE2 HIS A 592 −5.204 19.393 24.135 1.00 27.94 ATOM451 C HIS A 592 −3.937 18.295 28.377 1.00 20.49 ATOM 452 O HIS A 592−3.034 17.848 27.661 1.00 19.49 ATOM 453 N GLU A 593 −3.765 19.33829.184 1.00 19.12 ATOM 454 CA GLU A 593 −2.481 20.019 29.279 1.00 18.26ATOM 455 CB GLU A 593 −2.592 21.243 30.192 1.00 23.02 ATOM 456 CG GLU A593 −1.267 21.957 30.416 1.00 32.52 ATOM 457 CD GLU A 593 −1.422 23.29631.116 1.00 44.01 ATOM 458 OE1 GLU A 593 −2.062 24.200 30.535 1.00 41.08ATOM 459 OE2 GLU A 593 −0.901 23.446 32.244 1.00 45.85 ATOM 460 C GLU A593 −1.381 19.099 29.793 1.00 18.42 ATOM 461 O GLU A 593 −0.230 19.19529.365 1.00 16.87 ATOM 462 N VAL A 594 −1.738 18.209 30.710 1.00 18.22ATOM 463 CA VAL A 594 −0.770 17.275 31.277 1.00 17.13 ATOM 464 CB VAL A594 −1.372 16.506 32.465 1.00 16.16 ATOM 465 CG1 VAL A 594 −0.314 15.60533.085 1.00 20.37 ATOM 466 CG2 VAL A 594 −1.911 17.481 33.491 1.00 22.54ATOM 467 C VAL A 594 −0.299 16.263 30.235 1.00 15.25 ATOM 468 O VAL A594 0.902 16.005 30.101 1.00 16.26 ATOM 469 N LEU A 595 −1.246 15.68129.504 1.00 13.83 ATOM 470 CA LEU A 595 −0.897 14.705 28.478 1.00 14.01ATOM 471 CB LEU A 595 −2.163 14.147 27.818 1.00 9.50 ATOM 472 CG LEU A595 −1.969 13.167 26.653 1.00 18.45 ATOM 473 CD1 LEU A 595 −1.068 12.01427.076 1.00 12.38 ATOM 474 CD2 LEU A 595 −3.318 12.643 26.201 1.00 14.12ATOM 475 C LEU A 595 −0.002 15.372 27.438 1.00 13.61 ATOM 476 O LEU A595 1.004 14.804 27.010 1.00 13.98 ATOM 477 N CYS A 596 −0.358 16.58827.037 1.00 14.70 ATOM 478 CA CYS A 596 0.448 17.303 26.058 1.00 12.24ATOM 479 CB CYS A 596 −0.191 18.649 25.709 1.00 15.21 ATOM 480 SG CYS A596 −1.702 18.507 24.749 1.00 17.45 ATOM 481 C CYS A 596 1.861 17.53426.586 1.00 12.70 ATOM 482 O CYS A 596 2.839 17.327 25.868 1.00 11.06ATOM 483 N ARG A 597 1.970 17.959 27.841 1.00 11.36 ATOM 484 CA ARG A597 3.283 18.211 28.420 1.00 11.51 ATOM 485 CB ARG A 597 3.141 18.83629.815 1.00 14.74 ATOM 486 CG ARG A 597 4.463 19.343 30.388 1.00 15.86ATOM 487 CD ARG A 597 4.294 20.067 31.727 1.00 20.22 ATOM 488 NE ARG A597 3.565 21.332 31.614 1.00 21.93 ATOM 489 CZ ARG A 597 2.279 21.49331.916 1.00 27.00 ATOM 490 NH1 ARG A 597 1.560 20.469 32.357 1.00 22.77ATOM 491 NH2 ARG A 597 1.708 22.683 31.782 1.00 30.27 ATOM 492 C ARG A597 4.100 16.919 28.494 1.00 11.80 ATOM 493 O ARG A 597 5.287 16.90928.162 1.00 10.48 ATOM 494 N TRP A 598 3.454 15.830 28.905 1.00 11.97ATOM 495 CA TRP A 598 4.112 14.530 29.022 1.00 9.62 ATOM 496 CB TRP A598 3.125 13.488 29.556 1.00 11.57 ATOM 497 CG TRP A 598 3.717 12.11029.702 1.00 10.65 ATOM 498 CD2 TRP A 598 3.609 11.028 28.771 1.00 9.66ATOM 499 CE2 TRP A 598 4.350 9.948 29.298 1.00 8.24 ATOM 500 CE3 TRP A598 2.964 10.866 27.541 1.00 11.87 ATOM 501 CD1 TRP A 598 4.494 11.65630.728 1.00 9.74 ATOM 502 NE1 TRP A 598 4.878 10.359 30.492 1.00 11.42ATOM 503 CZ2 TRP A 598 4.459 8.720 28.635 1.00 7.38 ATOM 504 CZ3 TRP A598 3.075 9.646 26.886 1.00 9.43 ATOM 505 CH2 TRP A 598 3.818 8.59327.434 1.00 10.02 ATOM 506 C TRP A 598 4.656 14.064 27.670 1.00 12.66ATOM 507 O TRP A 598 5.804 13.617 27.568 1.00 11.33 ATOM 508 N ILE A 5993.823 14.160 26.637 1.00 9.84 ATOM 509 CA ILE A 599 4.232 13.748 25.2981.00 12.03 ATOM 510 CB ILE A 599 3.101 13.974 24.270 1.00 11.30 ATOM 511CG2 ILE A 599 3.648 13.807 22.856 1.00 13.41 ATOM 512 CG1 ILE A 5991.953 13.000 24.546 1.00 13.16 ATOM 513 CD1 ILE A 599 0.732 13.21823.668 1.00 13.06 ATOM 514 C ILE A 599 5.460 14.533 24.855 1.00 14.21ATOM 515 O ILE A 599 6.414 13.969 24.308 1.00 11.47 ATOM 516 N LEU A 6005.439 15.839 25.094 1.00 14.33 ATOM 517 CA LEU A 600 6.566 16.670 24.7071.00 13.61 ATOM 518 CB LEU A 600 6.214 18.151 24.882 1.00 13.53 ATOM 519CG LEU A 600 5.073 18.621 23.971 1.00 12.80 ATOM 520 CD1 LEU A 600 4.65220.036 24.336 1.00 15.66 ATOM 521 CD2 LEU A 600 5.518 18.557 22.520 1.0013.09 ATOM 522 C LEU A 600 7.800 16.297 25.523 1.00 10.78 ATOM 523 O LEUA 600 8.917 16.324 25.011 1.00 10.47 ATOM 524 N SER A 601 7.601 15.92526.788 1.00 10.50 ATOM 525 CA SER A 601 8.734 15.540 27.624 1.00 8.54ATOM 526 CB SER A 601 8.303 15.398 29.085 1.00 9.00 ATOM 527 OG SER A601 8.036 16.678 29.634 1.00 9.87 ATOM 528 C SER A 601 9.342 14.23927.129 1.00 9.99 ATOM 529 O SER A 601 10.563 14.082 27.104 1.00 10.43ATOM 530 N VAL A 602 8.487 13.300 26.739 1.00 10.77 ATOM 531 CA VAL A602 8.968 12.024 26.223 1.00 10.98 ATOM 532 CB VAL A 602 7.791 11.08125.874 1.00 12.52 ATOM 533 CG1 VAL A 602 8.303 9.856 25.138 1.00 9.22ATOM 534 CG2 VAL A 602 7.068 10.658 27.152 1.00 11.71 ATOM 535 C VAL A602 9.794 12.290 24.967 1.00 12.57 ATOM 536 O VAL A 602 10.935 11.84824.855 1.00 11.99 ATOM 537 N LYS A 603 9.220 13.043 24.034 1.00 12.97ATOM 538 CA LYS A 603 9.906 13.363 22.792 1.00 11.73 ATOM 539 CB LYS A603 9.025 14.268 21.928 1.00 14.00 ATOM 540 CG LYS A 603 9.666 14.68820.620 1.00 14.56 ATOM 541 CD LYS A 603 8.656 15.317 19.686 1.00 16.82ATOM 542 CE LYS A 603 8.088 16.603 20.262 1.00 24.97 ATOM 543 NZ LYS A603 7.169 17.256 19.300 1.00 39.23 ATOM 544 C LYS A 603 11.256 14.03523.042 1.00 11.50 ATOM 545 O LYS A 603 12.252 13.694 22.414 1.00 14.04ATOM 546 N LYS A 604 11.279 14.985 23.968 1.00 11.12 ATOM 547 CA LYS A604 12.501 15.714 24.293 1.00 13.84 ATOM 548 CB LYS A 604 12.181 16.84925.274 1.00 16.59 ATOM 549 CG LYS A 604 13.403 17.589 25.788 1.00 18.98ATOM 550 CD LYS A 604 13.016 18.673 26.784 1.00 25.53 ATOM 551 CE LYS A604 14.251 19.335 27.391 1.00 31.51 ATOM 552 NZ LYS A 604 13.893 20.35128.424 1.00 29.80 ATOM 553 C LYS A 604 13.582 14.824 24.890 1.00 12.98ATOM 554 O LYS A 604 14.776 15.073 24.710 1.00 13.10 ATOM 555 N ASN A605 13.173 13.773 25.587 1.00 12.62 ATOM 556 CA ASN A 605 14.146 12.90126.220 1.00 13.04 ATOM 557 CB ASN A 605 13.555 12.336 27.507 1.00 13.13ATOM 558 CG ASN A 605 13.579 13.356 28.638 1.00 32.58 ATOM 559 OD1 ASN A605 14.638 13.650 29.197 1.00 25.76 ATOM 560 ND2 ASN A 605 12.418 13.91828.962 1.00 30.95 ATOM 561 C ASN A 605 14.757 11.809 25.352 1.00 15.12ATOM 562 O ASN A 605 15.342 10.848 25.858 1.00 18.48 ATOM 563 N TYR A606 14.612 11.961 24.042 1.00 10.60 ATOM 564 CA TYR A 606 15.233 11.05123.093 1.00 10.45 ATOM 565 CB TYR A 606 14.254 10.645 21.982 1.00 10.34ATOM 566 CG TYR A 606 13.420 9.444 22.358 1.00 11.02 ATOM 567 CD1 TYR A606 13.950 8.156 22.297 1.00 8.31 ATOM 568 CE1 TYR A 606 13.222 7.06122.752 1.00 8.28 ATOM 569 CD2 TYR A 606 12.139 9.601 22.874 1.00 12.47ATOM 570 CE2 TYR A 606 11.410 8.516 23.335 1.00 15.05 ATOM 571 CZ TYR A606 11.955 7.252 23.275 1.00 15.46 ATOM 572 OH TYR A 606 11.227 6.18823.773 1.00 12.36 ATOM 573 C TYR A 606 16.362 11.908 22.539 1.00 11.41ATOM 574 O TYR A 606 16.216 13.129 22.428 1.00 14.91 ATOM 575 N ARG A607 17.499 11.293 22.234 1.00 11.41 ATOM 576 CA ARG A 607 18.627 12.04221.700 1.00 10.90 ATOM 577 CB ARG A 607 19.933 11.322 22.034 1.00 12.68ATOM 578 CG ARG A 607 20.078 11.019 23.520 1.00 10.36 ATOM 579 CD ARG A607 21.460 10.489 23.870 1.00 13.25 ATOM 580 NE ARG A 607 21.492 9.92925.221 1.00 9.55 ATOM 581 CZ ARG A 607 22.601 9.556 25.854 1.00 18.33ATOM 582 NH1 ARG A 607 23.781 9.686 25.262 1.00 13.50 ATOM 583 NH2 ARG A607 22.530 9.045 27.077 1.00 17.68 ATOM 584 C ARG A 607 18.425 12.15020.194 1.00 10.45 ATOM 585 O ARG A 607 18.616 11.182 19.458 1.00 12.53ATOM 586 N LYS A 608 18.052 13.340 19.738 1.00 11.88 ATOM 587 CA LYS A608 17.755 13.555 18.323 1.00 13.33 ATOM 588 CB LYS A 608 17.273 14.99318.104 1.00 18.33 ATOM 589 CG LYS A 608 18.226 16.064 18.574 1.00 34.41ATOM 590 CD LYS A 608 17.558 17.429 18.538 1.00 39.16 ATOM 591 CE LYS A608 18.430 18.485 19.193 1.00 44.56 ATOM 592 NZ LYS A 608 19.755 18.59518.525 1.00 49.34 ATOM 593 C LYS A 608 18.837 13.220 17.311 1.00 13.41ATOM 594 O LYS A 608 18.527 12.904 16.164 1.00 14.71 ATOM 595 N ASN A609 20.098 13.272 17.724 1.00 12.65 ATOM 596 CA ASN A 609 21.185 12.97716.804 1.00 15.37 ATOM 597 CB ASN A 609 22.383 13.872 17.121 1.00 19.55ATOM 598 CG ASN A 609 22.059 15.347 16.952 1.00 21.29 ATOM 599 OD1 ASN A609 21.630 15.779 15.882 1.00 28.72 ATOM 600 ND2 ASN A 609 22.261 16.12618.009 1.00 36.76 ATOM 601 C ASN A 609 21.593 11.507 16.743 1.00 14.47ATOM 602 O ASN A 609 22.486 11.135 15.981 1.00 15.29 ATOM 603 N VAL A610 20.955 10.670 17.557 1.00 11.89 ATOM 604 CA VAL A 610 21.221 9.23317.511 1.00 11.43 ATOM 605 CB VAL A 610 20.696 8.531 18.777 1.00 11.38ATOM 606 CG1 VAL A 610 20.649 7.019 18.571 1.00 10.56 ATOM 607 CG2 VAL A610 21.608 8.882 19.955 1.00 10.47 ATOM 608 C VAL A 610 20.432 8.80916.272 1.00 12.97 ATOM 609 O VAL A 610 19.221 9.025 16.198 1.00 11.59ATOM 610 N ALA A 611 21.131 8.223 15.302 1.00 11.37 ATOM 611 CA ALA A611 20.554 7.833 14.018 1.00 12.77 ATOM 612 CB ALA A 611 21.579 7.02113.223 1.00 12.83 ATOM 613 C ALA A 611 19.208 7.117 13.981 1.00 12.88ATOM 614 O ALA A 611 18.305 7.522 13.247 1.00 14.79 ATOM 615 N TYR A 61219.071 6.050 14.756 1.00 12.18 ATOM 616 CA TYR A 612 17.830 5.288 14.7431.00 10.69 ATOM 617 CB TYR A 612 18.147 3.824 14.408 1.00 13.15 ATOM 618CG TYR A 612 16.968 2.877 14.509 1.00 12.63 ATOM 619 CD1 TYR A 61215.832 3.054 13.729 1.00 19.45 ATOM 620 CE1 TYR A 612 14.752 2.18513.833 1.00 24.00 ATOM 621 CD2 TYR A 612 16.996 1.805 15.392 1.00 13.47ATOM 622 CE2 TYR A 612 15.930 0.938 15.503 1.00 24.95 ATOM 623 CZ TYR A612 14.812 1.129 14.722 1.00 24.27 ATOM 624 OH TYR A 612 13.761 0.24514.831 1.00 25.94 ATOM 625 C TYR A 612 17.017 5.371 16.028 1.00 11.05ATOM 626 O TYR A 612 15.812 5.632 15.989 1.00 9.25 ATOM 627 N HIS A 61317.667 5.159 17.166 1.00 10.71 ATOM 628 CA HIS A 613 16.951 5.199 18.4321.00 9.46 ATOM 629 CB HIS A 613 17.694 4.391 19.499 1.00 12.29 ATOM 630CG HIS A 613 17.706 2.923 19.232 1.00 13.22 ATOM 631 CD2 HIS A 61316.742 1.983 19.364 1.00 13.53 ATOM 632 ND1 HIS A 613 18.811 2.26218.726 1.00 8.83 ATOM 633 CE1 HIS A 613 18.523 0.989 18.562 1.00 12.86ATOM 634 NE2 HIS A 613 17.268 0.789 18.942 1.00 16.65 ATOM 635 C HIS A613 16.686 6.606 18.936 1.00 11.81 ATOM 636 O HIS A 613 17.226 7.02319.957 1.00 11.26 ATOM 637 N ASN A 614 15.859 7.333 18.192 1.00 12.20ATOM 638 CA ASN A 614 15.459 8.685 18.556 1.00 11.65 ATOM 639 CB ASN A614 15.955 9.702 17.516 1.00 19.08 ATOM 640 CG ASN A 614 15.631 9.29516.090 1.00 17.63 ATOM 641 OD1 ASN A 614 16.529 9.151 15.253 1.00 16.40ATOM 642 ND2 ASN A 614 14.349 9.115 15.802 1.00 11.39 ATOM 643 C ASN A614 13.933 8.690 18.644 1.00 11.53 ATOM 644 O ASN A 614 13.298 7.64718.493 1.00 9.32 ATOM 645 N TRP A 615 13.342 9.850 18.890 1.00 8.95 ATOM646 CA TRP A 615 11.893 9.929 19.015 1.00 9.02 ATOM 647 CB TRP A 61511.457 11.397 19.127 1.00 9.00 ATOM 648 CG TRP A 615 10.002 11.63818.809 1.00 8.75 ATOM 649 CD2 TRP A 615 8.860 11.228 19.581 1.00 10.58ATOM 650 CE2 TRP A 615 7.709 11.655 18.883 1.00 12.68 ATOM 651 CE3 TRP A615 8.698 10.542 20.789 1.00 12.70 ATOM 652 CD1 TRP A 615 9.504 12.27917.709 1.00 11.21 ATOM 653 NE1 TRP A 615 8.132 12.292 17.747 1.00 11.25ATOM 654 CZ2 TRP A 615 6.414 11.418 19.354 1.00 12.28 ATOM 655 CZ3 TRP A615 7.410 10.307 21.255 1.00 18.15 ATOM 656 CH2 TRP A 615 6.286 10.74420.536 1.00 13.05 ATOM 657 C TRP A 615 11.090 9.237 17.910 1.00 8.08ATOM 658 O TRP A 615 10.093 8.579 18.197 1.00 9.24 ATOM 659 N ARG A 61611.514 9.365 16.656 1.00 9.61 ATOM 660 CA ARG A 616 10.750 8.759 15.5701.00 11.24 ATOM 661 CB ARG A 616 11.346 9.129 14.206 1.00 9.33 ATOM 662CG ARG A 616 11.241 10.630 13.885 1.00 13.33 ATOM 663 CD ARG A 616 9.81711.169 14.120 1.00 11.22 ATOM 664 NE ARG A 616 9.705 12.598 13.823 1.0013.61 ATOM 665 CZ ARG A 616 9.119 13.103 12.741 1.00 15.86 ATOM 666 NH1ARG A 616 8.577 12.300 11.834 1.00 15.89 ATOM 667 NH2 ARG A 616 9.07314.419 12.564 1.00 19.53 ATOM 668 C ARG A 616 10.607 7.250 15.705 1.009.88 ATOM 669 O ARG A 616 9.575 6.692 15.328 1.00 10.40 ATOM 670 N HIS A617 11.625 6.582 16.242 1.00 7.87 ATOM 671 CA HIS A 617 11.514 5.14116.419 1.00 7.37 ATOM 672 CB HIS A 617 12.862 4.523 16.782 1.00 11.98ATOM 673 CG HIS A 617 12.742 3.163 17.390 1.00 8.70 ATOM 674 CD2 HIS A617 13.043 2.715 18.632 1.00 9.51 ATOM 675 ND1 HIS A 617 12.206 2.08816.713 1.00 8.99 ATOM 676 CE1 HIS A 617 12.183 1.036 17.510 1.00 11.83ATOM 677 NE2 HIS A 617 12.684 1.391 18.681 1.00 10.58 ATOM 678 C HIS A617 10.488 4.816 17.506 1.00 8.63 ATOM 679 O HIS A 617 9.692 3.88817.361 1.00 10.24 ATOM 680 N ALA A 618 10.498 5.586 18.591 1.00 7.45ATOM 681 CA ALA A 618 9.549 5.358 19.687 1.00 8.54 ATOM 682 CB ALA A 6189.887 6.261 20.864 1.00 11.31 ATOM 683 C ALA A 618 8.126 5.637 19.2101.00 8.39 ATOM 684 O ALA A 618 7.184 4.900 19.523 1.00 9.03 ATOM 685 NPHE A 619 7.981 6.725 18.465 1.00 8.88 ATOM 686 CA PHE A 619 6.695 7.11817.911 1.00 9.63 ATOM 687 CB PHE A 619 6.850 8.418 17.119 1.00 12.92ATOM 688 CG PHE A 619 5.618 8.809 16.357 1.00 10.44 ATOM 689 CD1 PHE A619 4.432 9.066 17.021 1.00 18.21 ATOM 690 CD2 PHE A 619 5.646 8.91414.974 1.00 12.41 ATOM 691 CE1 PHE A 619 3.291 9.412 16.324 1.00 14.74ATOM 692 CE2 PHE A 619 4.508 9.260 14.270 1.00 13.16 ATOM 693 CZ PHE A619 3.328 9.512 14.947 1.00 11.01 ATOM 694 C PHE A 619 6.150 6.01716.996 1.00 9.52 ATOM 695 O PHE A 619 4.975 5.654 17.079 1.00 9.30 ATOM696 N ASN A 620 7.001 5.490 16.119 1.00 10.15 ATOM 697 CA ASN A 6206.583 4.428 15.204 1.00 11.34 ATOM 698 CB ASN A 620 7.694 4.123 14.1941.00 9.10 ATOM 699 CG ASN A 620 7.658 5.052 12.999 1.00 17.16 ATOM 700OD1 ASN A 620 8.665 5.656 12.634 1.00 19.51 ATOM 701 ND2 ASN A 620 6.4905.166 12.382 1.00 12.88 ATOM 702 C ASN A 620 6.206 3.161 15.956 1.009.23 ATOM 703 O ASN A 620 5.273 2.457 15.574 1.00 10.76 ATOM 704 N THR A621 6.936 2.871 17.026 1.00 8.56 ATOM 705 CA THR A 621 6.650 1.68817.819 1.00 9.52 ATOM 706 CB THR A 621 7.707 1.509 18.928 1.00 8.96 ATOM707 OG1 THR A 621 9.010 1.404 18.328 1.00 9.14 ATOM 708 CG2 THR A 6217.428 0.244 19.736 1.00 7.93 ATOM 709 C THR A 621 5.252 1.821 18.4251.00 10.48 ATOM 710 O THR A 621 4.455 0.879 18.382 1.00 10.11 ATOM 711 NALA A 622 4.954 2.995 18.978 1.00 8.32 ATOM 712 CA ALA A 622 3.644 3.24419.573 1.00 9.28 ATOM 713 CB ALA A 622 3.642 4.583 20.294 1.00 9.90 ATOM714 C ALA A 622 2.567 3.224 18.488 1.00 10.02 ATOM 715 O ALA A 622 1.4472.769 18.721 1.00 8.06 ATOM 716 N GLN A 623 2.902 3.708 17.297 1.00 7.82ATOM 717 CA GLN A 623 1.927 3.708 16.211 1.00 10.17 ATOM 718 CB GLN A623 2.456 4.487 15.003 1.00 8.39 ATOM 719 CG GLN A 623 1.473 4.57813.825 1.00 8.23 ATOM 720 CD GLN A 623 1.444 3.319 12.967 1.00 13.63ATOM 721 OE1 GLN A 623 2.484 2.730 12.682 1.00 12.75 ATOM 722 NE2 GLN A623 0.258 2.919 12.535 1.00 11.69 ATOM 723 C GLN A 623 1.597 2.27815.806 1.00 10.35 ATOM 724 O GLN A 623 0.449 1.962 15.501 1.00 9.61 ATOM725 N CYS A 624 2.601 1.406 15.802 1.00 9.08 ATOM 726 CA CYS A 624 2.3550.017 15.439 1.00 9.34 ATOM 727 CB CYS A 624 3.679 −0.740 15.273 1.0011.00 ATOM 728 SG CYS A 624 3.481 −2.446 14.713 1.00 11.71 ATOM 729 CCYS A 624 1.495 −0.625 16.529 1.00 10.17 ATOM 730 O CYS A 624 0.631−1.448 16.239 1.00 10.64 ATOM 731 N MET A 625 1.728 −0.238 17.781 1.009.06 ATOM 732 CA MET A 625 0.933 −0.764 18.892 1.00 9.38 ATOM 733 CB META 625 1.418 −0.180 20.225 1.00 8.21 ATOM 734 CG MET A 625 0.692 −0.71821.466 1.00 8.16 ATOM 735 SD MET A 625 0.904 −2.512 21.728 1.00 11.88ATOM 736 CE MET A 625 2.600 −2.586 22.309 1.00 11.24 ATOM 737 C MET A625 −0.529 −0.376 18.661 1.00 9.31 ATOM 738 O MET A 625 −1.434 −1.20818.757 1.00 10.06 ATOM 739 N PHE A 626 −0.757 0.896 18.353 1.00 9.47ATOM 740 CA PHE A 626 −2.112 1.377 18.092 1.00 9.60 ATOM 741 CB PHE A626 −2.077 2.859 17.725 1.00 9.70 ATOM 742 CG PHE A 626 −3.432 3.45117.461 1.00 7.25 ATOM 743 CD1 PHE A 626 −4.241 3.858 18.509 1.00 13.86ATOM 744 CD2 PHE A 626 −3.897 3.598 16.163 1.00 13.47 ATOM 745 CE1 PHE A626 −5.491 4.411 18.267 1.00 18.88 ATOM 746 CE2 PHE A 626 −5.144 4.14715.917 1.00 11.81 ATOM 747 CZ PHE A 626 −5.942 4.552 16.970 1.00 16.53ATOM 748 C PHE A 626 −2.737 0.579 16.940 1.00 10.98 ATOM 749 O PHE A 626−3.862 0.084 17.047 1.00 12.71 ATOM 750 N ALA A 627 −1.999 0.455 15.8381.00 7.24 ATOM 751 CA ALA A 627 −2.486 −0.279 14.675 1.00 9.31 ATOM 752CB ALA A 627 −1.454 −0.220 13.549 1.00 14.42 ATOM 753 C ALA A 627 −2.803−1.734 15.024 1.00 11.79 ATOM 754 O ALA A 627 −3.815 −2.276 14.583 1.0011.59 ATOM 755 N ALA A 628 −1.945 −2.361 15.824 1.00 10.63 ATOM 756 CAALA A 628 −2.158 −3.749 16.219 1.00 11.00 ATOM 757 CB ALA A 628 −0.934−4.280 16.961 1.00 11.43 ATOM 758 C ALA A 628 −3.398 −3.877 17.099 1.0011.16 ATOM 759 O ALA A 628 −4.152 −4.845 16.994 1.00 12.30 ATOM 760 NLEU A 629 −3.608 −2.896 17.970 1.00 9.63 ATOM 761 CA LEU A 629 −4.765−2.924 18.856 1.00 9.96 ATOM 762 CB LEU A 629 −4.627 −1.858 19.945 1.0012.79 ATOM 763 CG LEU A 629 −3.538 −2.115 20.990 1.00 10.87 ATOM 764 CD1LEU A 629 −3.286 −0.859 21.792 1.00 11.38 ATOM 765 CD2 LEU A 629 −3.956−3.264 21.897 1.00 14.99 ATOM 766 C LEU A 629 −6.051 −2.692 18.073 1.0012.31 ATOM 767 O LEU A 629 −7.084 −3.300 18.364 1.00 11.63 ATOM 768 NLYS A 630 −5.973 −1.822 17.070 1.00 11.64 ATOM 769 CA LYS A 630 −7.125−1.479 16.242 1.00 12.87 ATOM 770 CB LYS A 630 −6.984 −0.037 15.738 1.0015.53 ATOM 771 CG LYS A 630 −7.084 1.030 16.820 1.00 13.30 ATOM 772 CDLYS A 630 −8.495 1.104 17.385 1.00 19.60 ATOM 773 CE LYS A 630 −8.6982.349 18.245 1.00 18.93 ATOM 774 NZ LYS A 630 −7.877 2.334 19.481 1.0040.94 ATOM 775 C LYS A 630 −7.323 −2.422 15.049 1.00 13.54 ATOM 776 OLYS A 630 −8.122 −3.350 15.107 1.00 12.81 ATOM 777 N ALA A 631 −6.597−2.170 13.967 1.00 13.05 ATOM 778 CA ALA A 631 −6.701 −2.997 12.770 1.0014.94 ATOM 779 CB ALA A 631 −5.763 −2.460 11.688 1.00 17.58 ATOM 780 CALA A 631 −6.374 −4.461 13.068 1.00 16.22 ATOM 781 O ALA A 631 −6.960−5.375 12.479 1.00 15.44 ATOM 782 N GLY A 632 −5.439 −4.670 13.990 1.0012.88 ATOM 783 CA GLY A 632 −5.028 −6.014 14.359 1.00 13.10 ATOM 784 CGLY A 632 −5.995 −6.711 15.298 1.00 13.12 ATOM 785 O GLY A 632 −5.850−7.902 15.576 1.00 15.03 ATOM 786 N LYS A 633 −6.968 −5.959 15.803 1.0013.75 ATOM 787 CA LYS A 633 −7.997 −6.497 16.692 1.00 14.20 ATOM 788 CBLYS A 633 −8.815 −7.566 15.954 1.00 13.72 ATOM 789 CG LYS A 633 −9.438−7.109 14.631 1.00 23.64 ATOM 790 CD LYS A 633 −10.532 −6.072 14.8341.00 30.20 ATOM 791 CE LYS A 633 −11.182 −5.672 13.510 1.00 34.87 ATOM792 NZ LYS A 633 −10.227 −4.989 12.594 1.00 46.21 ATOM 793 C LYS A 633−7.464 −7.085 17.997 1.00 14.18 ATOM 794 O LYS A 633 −8.048 −8.02418.540 1.00 14.72 ATOM 795 N ILE A 634 −6.366 −6.536 18.507 1.00 13.07ATOM 796 CA ILE A 634 −5.801 −7.037 19.755 1.00 12.44 ATOM 797 CB ILE A634 −4.262 −6.819 19.799 1.00 13.52 ATOM 798 CG2 ILE A 634 −3.709 −7.23621.156 1.00 14.73 ATOM 799 CG1 ILE A 634 −3.581 −7.632 18.694 1.00 14.10ATOM 800 CD1 ILE A 634 −3.757 −9.128 18.829 1.00 14.44 ATOM 801 C ILE A634 −6.439 −6.346 20.967 1.00 12.23 ATOM 802 O ILE A 634 −6.456 −6.89422.067 1.00 12.06 ATOM 803 N GLN A 635 −6.990 −5.155 20.752 1.00 13.17ATOM 804 CA GLN A 635 −7.597 −4.377 21.834 1.00 12.59 ATOM 805 CB GLN A635 −8.330 −3.158 21.267 1.00 14.77 ATOM 806 CG GLN A 635 −8.796 −2.18022.345 1.00 17.07 ATOM 807 CD GLN A 635 −9.479 −0.949 21.778 1.00 17.87ATOM 808 OE1 GLN A 635 −9.080 −0.425 20.741 1.00 15.93 ATOM 809 NE2 GLNA 635 −10.509 −0.473 22.471 1.00 27.59 ATOM 810 C GLN A 635 −8.549−5.127 22.762 1.00 13.46 ATOM 811 O GLN A 635 −8.382 −5.107 23.984 1.0012.66 ATOM 812 N ASN A 636 −9.554 −5.778 22.188 1.00 12.36 ATOM 813 CAASN A 636 −10.533 −6.493 22.996 1.00 15.16 ATOM 814 CB ASN A 636 −11.736−6.872 22.130 1.00 13.54 ATOM 815 CG ASN A 636 −12.508 −5.655 21.6581.00 19.96 ATOM 816 OD1 ASN A 636 −12.211 −4.526 22.059 1.00 19.43 ATOM817 ND2 ASN A 636 −13.506 −5.874 20.810 1.00 20.88 ATOM 818 C ASN A 636−10.002 −7.708 23.743 1.00 14.39 ATOM 819 O ASN A 636 −10.720 −8.31224.539 1.00 17.61 ATOM 820 N LYS A 637 −8.744 −8.060 23.500 1.00 13.69ATOM 821 CA LYS A 637 −8.132 −9.194 24.180 1.00 13.94 ATOM 822 CB LYS A637 −7.124 −9.893 23.262 1.00 13.19 ATOM 823 CG LYS A 637 −7.667 −10.32821.910 1.00 16.41 ATOM 824 CD LYS A 637 −6.599 −11.079 21.128 1.00 18.79ATOM 825 CE LYS A 637 −7.110 −11.542 19.773 1.00 21.00 ATOM 826 NZ LYS A637 −8.266 −12.467 19.893 1.00 27.72 ATOM 827 C LYS A 637 −7.400 −8.70825.435 1.00 14.29 ATOM 828 O LYS A 637 −6.930 −9.514 26.237 1.00 15.91ATOM 829 N LEU A 638 −7.316 −7.391 25.611 1.00 13.88 ATOM 830 CA LEU A638 −6.602 −6.828 26.757 1.00 14.02 ATOM 831 CB LEU A 638 −5.426 −5.98826.256 1.00 14.42 ATOM 832 CG LEU A 638 −4.496 −6.595 25.201 1.00 13.65ATOM 833 CD1 LEU A 638 −3.405 −5.589 24.860 1.00 13.98 ATOM 834 CD2 LEUA 638 −3.881 −7.885 25.718 1.00 12.70 ATOM 835 C LEU A 638 −7.464 −5.97327.687 1.00 13.83 ATOM 836 O LEU A 638 −8.551 −5.529 27.313 1.00 16.24ATOM 837 N THR A 639 −6.968 −5.745 28.902 1.00 13.04 ATOM 838 CA THR A639 −7.665 −4.913 29.885 1.00 12.97 ATOM 839 CB THR A 639 −7.225 −5.24431.323 1.00 9.72 ATOM 840 OG1 THR A 639 −5.883 −4.777 31.534 1.00 11.58ATOM 841 CG2 THR A 639 −7.284 −6.752 31.574 1.00 13.01 ATOM 842 C THR A639 −7.320 −3.443 29.627 1.00 11.14 ATOM 843 O THR A 639 −6.369 −3.14728.910 1.00 12.39 ATOM 844 N ASP A 640 −8.082 −2.524 30.216 1.00 11.83ATOM 845 CA ASP A 640 −7.814 −1.098 30.027 1.00 11.03 ATOM 846 CB ASP A640 −8.846 −0.243 30.774 1.00 9.58 ATOM 847 CG ASP A 640 −10.238 −0.36830.191 1.00 23.27 ATOM 848 OD1 ASP A 640 −10.357 −0.828 29.037 1.0021.74 ATOM 849 OD2 ASP A 640 −11.211 0.011 30.879 1.00 18.96 ATOM 850 CASP A 640 −6.419 −0.724 30.519 1.00 10.85 ATOM 851 O ASP A 640 −5.7080.058 29.881 1.00 11.05 ATOM 852 N LEU A 641 −6.031 −1.290 31.655 1.0011.16 ATOM 853 CA LEU A 641 −4.727 −1.004 32.235 1.00 10.51 ATOM 854 CBLEU A 641 −4.628 −1.606 33.640 1.00 13.05 ATOM 855 CG LEU A 641 −5.633−1.081 34.674 1.00 13.28 ATOM 856 CD1 LEU A 641 −5.383 −1.762 36.0051.00 14.91 ATOM 857 CD2 LEU A 641 −5.506 0.432 34.813 1.00 12.98 ATOM858 C LEU A 641 −3.593 −1.527 31.359 1.00 10.02 ATOM 859 O LEU A 641−2.550 −0.883 31.237 1.00 9.79 ATOM 860 N GLU A 642 −3.791 −2.692 30.7481.00 9.49 ATOM 861 CA GLU A 642 −2.756 −3.253 29.886 1.00 9.55 ATOM 862CB GLU A 642 −3.120 −4.687 29.493 1.00 13.24 ATOM 863 CG GLU A 642−3.215 −5.605 30.705 1.00 17.56 ATOM 864 CD GLU A 642 −3.645 −7.02130.373 1.00 14.47 ATOM 865 OE1 GLU A 642 −4.411 −7.212 29.404 1.00 12.63ATOM 866 OE2 GLU A 642 −3.233 −7.949 31.108 1.00 15.36 ATOM 867 C GLU A642 −2.568 −2.366 28.656 1.00 9.56 ATOM 868 O GLU A 642 −1.442 −2.13528.217 1.00 10.36 ATOM 869 N ILE A 643 −3.665 −1.847 28.112 1.00 9.98ATOM 870 CA ILE A 643 −3.585 −0.978 26.945 1.00 11.53 ATOM 871 CB ILE A643 −4.992 −0.683 26.391 1.00 12.52 ATOM 872 CG2 ILE A 643 −4.915 0.36725.281 1.00 11.83 ATOM 873 CG1 ILE A 643 −5.614 −1.984 25.885 1.00 11.82ATOM 874 CD1 ILE A 643 −7.089 −1.872 25.553 1.00 18.49 ATOM 875 C ILE A643 −2.883 0.323 27.339 1.00 9.56 ATOM 876 O ILE A 643 −1.993 0.80626.635 1.00 10.76 ATOM 877 N LEU A 644 −3.278 0.880 28.479 1.00 9.68ATOM 878 CA LEU A 644 −2.663 2.105 28.974 1.00 9.78 ATOM 879 CB LEU A644 −3.285 2.482 30.321 1.00 11.15 ATOM 880 CG LEU A 644 −2.658 3.64331.093 1.00 14.02 ATOM 881 CD1 LEU A 644 −2.853 4.946 30.328 1.00 14.15ATOM 882 CD2 LEU A 644 −3.315 3.735 32.471 1.00 14.10 ATOM 883 C LEU A644 −1.152 1.899 29.139 1.00 9.98 ATOM 884 O LEU A 644 −0.342 2.72028.694 1.00 9.97 ATOM 885 N ALA A 645 −0.778 0.788 29.766 1.00 8.98 ATOM886 CA ALA A 645 0.634 0.492 30.008 1.00 8.84 ATOM 887 CB ALA A 6450.763 −0.724 30.928 1.00 8.17 ATOM 888 C ALA A 645 1.414 0.256 28.7181.00 9.39 ATOM 889 O ALA A 645 2.556 0.687 28.598 1.00 9.92 ATOM 890 NLEU A 646 0.799 −0.430 27.761 1.00 8.76 ATOM 891 CA LEU A 646 1.462−0.708 26.488 1.00 8.34 ATOM 892 CB LEU A 646 0.607 −1.652 25.644 1.0010.30 ATOM 893 CG LEU A 646 0.541 −3.101 26.128 1.00 11.47 ATOM 894 CD1LEU A 646 −0.557 −3.832 25.379 1.00 15.28 ATOM 895 CD2 LEU A 646 1.879−3.779 25.906 1.00 10.48 ATOM 896 C LEU A 646 1.761 0.550 25.682 1.007.55 ATOM 897 O LEU A 646 2.837 0.676 25.094 1.00 9.05 ATOM 898 N LEU A647 0.812 1.479 25.643 1.00 7.57 ATOM 899 CA LEU A 647 1.020 2.71324.889 1.00 8.87 ATOM 900 CB LEU A 647 −0.283 3.516 24.803 1.00 7.82ATOM 901 CG LEU A 647 −0.214 4.722 23.862 1.00 10.06 ATOM 902 CD1 LEU A647 0.194 4.251 22.470 1.00 13.81 ATOM 903 CD2 LEU A 647 −1.560 5.43723.820 1.00 12.05 ATOM 904 C LEU A 647 2.120 3.550 25.540 1.00 8.12 ATOM905 O LEU A 647 3.011 4.070 24.863 1.00 8.78 ATOM 906 N ILE A 648 2.0563.676 26.860 1.00 9.66 ATOM 907 CA ILE A 648 3.065 4.429 27.597 1.008.86 ATOM 908 CB ILE A 648 2.692 4.501 29.100 1.00 10.81 ATOM 909 CG2ILE A 648 3.851 5.063 29.917 1.00 7.70 ATOM 910 CG1 ILE A 648 1.4395.364 29.266 1.00 11.45 ATOM 911 CD1 ILE A 648 0.921 5.437 30.688 1.009.57 ATOM 912 C ILE A 648 4.427 3.756 27.424 1.00 8.38 ATOM 913 O ILE A648 5.439 4.427 27.180 1.00 9.63 ATOM 914 N ALA A 649 4.456 2.430 27.5361.00 9.32 ATOM 915 CA ALA A 649 5.710 1.697 27.388 1.00 9.98 ATOM 916 CBALA A 649 5.506 0.214 27.703 1.00 11.64 ATOM 917 C ALA A 649 6.285 1.85325.989 1.00 9.64 ATOM 918 O ALA A 649 7.471 2.126 25.831 1.00 10.34 ATOM919 N ALA A 650 5.449 1.680 24.971 1.00 11.02 ATOM 920 CA ALA A 6505.914 1.814 23.591 1.00 9.43 ATOM 921 CB ALA A 650 4.747 1.618 22.6171.00 8.79 ATOM 922 C ALA A 650 6.561 3.183 23.359 1.00 8.11 ATOM 923 OALA A 650 7.628 3.292 22.748 1.00 9.60 ATOM 924 N LEU A 651 5.914 4.23323.851 1.00 9.58 ATOM 925 CA LEU A 651 6.443 5.582 23.679 1.00 10.27ATOM 926 CB LEU A 651 5.383 6.613 24.066 1.00 9.84 ATOM 927 CG LEU A 6514.198 6.717 23.101 1.00 6.24 ATOM 928 CD1 LEU A 651 3.038 7.432 23.7721.00 14.57 ATOM 929 CD2 LEU A 651 4.637 7.463 21.846 1.00 11.43 ATOM 930C LEU A 651 7.706 5.848 24.488 1.00 10.46 ATOM 931 O LEU A 651 8.5736.611 24.066 1.00 9.75 ATOM 932 N SER A 652 7.807 5.194 25.640 1.00 9.58ATOM 933 CA SER A 652 8.935 5.394 26.542 1.00 10.30 ATOM 934 CB SER A652 8.422 5.453 27.983 1.00 9.30 ATOM 935 OG SER A 652 7.367 6.37928.133 1.00 11.78 ATOM 936 C SER A 652 10.026 4.334 26.504 1.00 8.64ATOM 937 O SER A 652 11.068 4.520 27.125 1.00 9.90 ATOM 938 N HIS A 6539.805 3.249 25.765 1.00 9.64 ATOM 939 CA HIS A 653 10.739 2.128 25.7691.00 9.99 ATOM 940 CB HIS A 653 10.164 0.963 24.952 1.00 8.26 ATOM 941CG HIS A 653 10.546 0.980 23.510 1.00 8.55 ATOM 942 CD2 HIS A 653 11.5290.333 22.842 1.00 9.53 ATOM 943 ND1 HIS A 653 9.881 1.740 22.569 1.0010.01 ATOM 944 CE1 HIS A 653 10.440 1.559 21.387 1.00 6.46 ATOM 945 NE2HIS A 653 11.444 0.708 21.526 1.00 6.65 ATOM 946 C HIS A 653 12.2102.321 25.412 1.00 10.62 ATOM 947 O HIS A 653 13.024 1.459 25.741 1.008.86 ATOM 948 N ASP A 654 12.559 3.424 24.752 1.00 9.82 ATOM 949 CA ASPA 654 13.959 3.673 24.406 1.00 9.46 ATOM 950 CB ASP A 654 14.184 3.58022.889 1.00 10.10 ATOM 951 CG ASP A 654 14.509 2.172 22.432 1.00 10.77ATOM 952 OD1 ASP A 654 15.159 1.444 23.204 1.00 9.55 ATOM 953 OD2 ASP A654 14.141 1.812 21.294 1.00 8.85 ATOM 954 C ASP A 654 14.477 5.02424.896 1.00 9.92 ATOM 955 O ASP A 654 15.500 5.507 24.413 1.00 9.67 ATOM956 N LEU A 655 13.783 5.619 25.865 1.00 9.19 ATOM 957 CA LEU A 65514.169 6.922 26.408 1.00 10.06 ATOM 958 CB LEU A 655 13.364 7.214 27.6771.00 8.55 ATOM 959 CG LEU A 655 11.900 7.603 27.479 1.00 10.24 ATOM 960CD1 LEU A 655 11.151 7.468 28.805 1.00 9.10 ATOM 961 CD2 LEU A 65511.819 9.028 26.944 1.00 15.71 ATOM 962 C LEU A 655 15.658 7.101 26.7131.00 10.50 ATOM 963 O LEU A 655 16.279 6.268 27.372 1.00 9.92 ATOM 964 NASP A 656 16.215 8.209 26.232 1.00 8.66 ATOM 965 CA ASP A 656 17.6228.542 26.448 1.00 8.66 ATOM 966 CB ASP A 656 17.867 8.811 27.941 1.0011.08 ATOM 967 CG ASP A 656 19.211 9.475 28.207 1.00 16.07 ATOM 968 OD1ASP A 656 19.576 10.406 27.460 1.00 11.04 ATOM 969 OD2 ASP A 656 19.8979.074 29.173 1.00 13.88 ATOM 970 C ASP A 656 18.600 7.483 25.939 1.008.59 ATOM 971 O ASP A 656 19.670 7.288 26.511 1.00 9.89 ATOM 972 N HIS A657 18.242 6.806 24.851 1.00 9.07 ATOM 973 CA HIS A 657 19.118 5.79024.284 1.00 10.63 ATOM 974 CB HIS A 657 18.412 5.068 23.137 1.00 9.06ATOM 975 CG HIS A 657 19.095 3.810 22.712 1.00 8.47 ATOM 976 CD2 HIS A657 20.347 3.589 22.245 1.00 7.97 ATOM 977 ND1 HIS A 657 18.480 2.57522.748 1.00 12.46 ATOM 978 CE1 HIS A 657 19.322 1.652 22.322 1.00 5.38ATOM 979 NE2 HIS A 657 20.464 2.242 22.011 1.00 12.33 ATOM 980 C HIS A657 20.404 6.453 23.778 1.00 11.40 ATOM 981 O HIS A 657 20.362 7.40422.993 1.00 11.45 ATOM 982 N PRO A 658 21.567 5.957 24.230 1.00 11.01ATOM 983 CD PRO A 658 21.697 4.963 25.311 1.00 10.94 ATOM 984 CA PRO A658 22.884 6.479 23.850 1.00 10.19 ATOM 985 CB PRO A 658 23.792 5.93024.944 1.00 9.66 ATOM 986 CG PRO A 658 23.171 4.618 25.252 1.00 16.61ATOM 987 C PRO A 658 23.386 6.123 22.451 1.00 11.02 ATOM 988 O PRO A 65824.428 6.627 22.021 1.00 12.41 ATOM 989 N GLY A 659 22.659 5.265 21.7441.00 8.82 ATOM 990 CA GLY A 659 23.080 4.888 20.405 1.00 8.78 ATOM 991 CGLY A 659 24.115 3.781 20.356 1.00 9.97 ATOM 992 O GLY A 659 24.7503.566 19.316 1.00 12.32 ATOM 993 N VAL A 660 24.305 3.095 21.480 1.008.93 ATOM 994 CA VAL A 660 25.248 1.983 21.564 1.00 9.69 ATOM 995 CB VALA 660 26.554 2.387 22.301 1.00 10.19 ATOM 996 CG1 VAL A 660 27.358 3.35521.434 1.00 12.07 ATOM 997 CG2 VAL A 660 26.236 3.020 23.642 1.00 12.93ATOM 998 C VAL A 660 24.545 0.834 22.289 1.00 10.76 ATOM 999 O VAL A 66023.601 1.059 23.052 1.00 10.23 ATOM 1000 N SER A 661 25.002 −0.39222.049 1.00 7.63 ATOM 1001 CA SER A 661 24.371 −1.577 22.624 1.00 10.33ATOM 1002 CB SER A 661 24.748 −2.801 21.793 1.00 8.76 ATOM 1003 OG SER A661 26.099 −3.151 22.021 1.00 9.56 ATOM 1004 C SER A 661 24.687 −1.86424.088 1.00 9.36 ATOM 1005 O SER A 661 25.549 −1.230 24.696 1.00 10.42ATOM 1006 N ASN A 662 23.969 −2.838 24.643 1.00 10.10 ATOM 1007 CA ASN A662 24.165 −3.261 26.026 1.00 8.94 ATOM 1008 CB ASN A 662 23.177 −4.36926.384 1.00 12.24 ATOM 1009 CG ASN A 662 21.832 −3.836 26.824 1.00 11.27ATOM 1010 OD1 ASN A 662 20.794 −4.457 26.592 1.00 19.20 ATOM 1011 ND2ASN A 662 21.844 −2.689 27.483 1.00 5.90 ATOM 1012 C ASN A 662 25.586−3.781 26.161 1.00 11.89 ATOM 1013 O ASN A 662 26.289 −3.459 27.116 1.0012.39 ATOM 1014 N GLN A 663 26.010 −4.598 25.199 1.00 10.34 ATOM 1015 CAGLN A 663 27.356 −5.139 25.246 1.00 11.06 ATOM 1016 CB GLN A 663 27.578−6.120 24.083 1.00 14.83 ATOM 1017 CG GLN A 663 26.677 −7.373 24.1971.00 25.28 ATOM 1018 CD GLN A 663 25.283 −7.191 23.575 1.00 24.96 ATOM1019 OE1 GLN A 663 24.919 −6.113 23.106 1.00 31.10 ATOM 1020 NE2 GLN A663 24.497 −8.271 23.572 1.00 46.85 ATOM 1021 C GLN A 663 28.422 −4.03925.236 1.00 13.51 ATOM 1022 O GLN A 663 29.439 −4.161 25.921 1.00 12.70ATOM 1023 N PHE A 664 28.184 −2.956 24.504 1.00 12.64 ATOM 1024 CA PHE A664 29.145 −1.852 24.465 1.00 11.20 ATOM 1025 CB PHE A 664 28.754 −0.83823.380 1.00 12.60 ATOM 1026 CG PHE A 664 29.669 0.355 23.296 1.00 15.21ATOM 1027 CD1 PHE A 664 29.554 1.407 24.198 1.00 13.93 ATOM 1028 CD2 PHEA 664 30.668 0.409 22.336 1.00 10.34 ATOM 1029 CE1 PHE A 664 30.4192.484 24.144 1.00 11.59 ATOM 1030 CE2 PHE A 664 31.541 1.487 22.275 1.0016.42 ATOM 1031 CZ PHE A 664 31.418 2.527 23.182 1.00 18.27 ATOM 1032 CPHE A 664 29.207 −1.171 25.830 1.00 11.75 ATOM 1033 O PHE A 664 30.290−0.818 26.306 1.00 11.28 ATOM 1034 N LEU A 665 28.046 −0.980 26.452 1.0011.17 ATOM 1035 CA LEU A 665 27.982 −0.346 27.768 1.00 11.46 ATOM 1036CB LEU A 665 26.524 −0.163 28.204 1.00 11.38 ATOM 1037 CG LEU A 66525.703 0.864 27.420 1.00 9.72 ATOM 1038 CD1 LEU A 665 24.304 0.95928.015 1.00 16.35 ATOM 1039 CD2 LEU A 665 26.399 2.215 27.470 1.00 13.26ATOM 1040 C LEU A 665 28.726 −1.200 28.793 1.00 13.75 ATOM 1041 O LEU A665 29.404 −0.686 29.681 1.00 11.85 ATOM 1042 N ILE A 666 28.591 −2.51228.661 1.00 12.41 ATOM 1043 CA ILE A 666 29.259 −3.444 29.559 1.00 13.52ATOM 1044 CB ILE A 666 28.773 −4.887 29.300 1.00 13.10 ATOM 1045 CG2 ILEA 666 29.667 −5.882 30.020 1.00 13.00 ATOM 1046 CG1 ILE A 666 27.322−5.036 29.761 1.00 10.73 ATOM 1047 CD1 ILE A 666 26.687 −6.346 29.3691.00 14.67 ATOM 1048 C ILE A 666 30.770 −3.381 29.356 1.00 11.71 ATOM1049 O ILE A 666 31.541 −3.297 30.317 1.00 14.40 ATOM 1050 N ASN A 66731.183 −3.408 28.094 1.00 12.52 ATOM 1051 CA ASN A 667 32.599 −3.38227.733 1.00 11.69 ATOM 1052 CB ASN A 667 32.745 −3.652 26.232 1.00 15.94ATOM 1053 CG ASN A 667 32.340 −5.065 25.848 1.00 13.91 ATOM 1054 OD1 ASNA 667 32.138 −5.363 24.669 1.00 17.63 ATOM 1055 ND2 ASN A 667 32.233−5.946 26.837 1.00 11.25 ATOM 1056 C ASN A 667 33.323 −2.090 28.091 1.0015.59 ATOM 1057 O ASN A 667 34.530 −2.104 28.355 1.00 16.72 ATOM 1058 NTHR A 668 32.601 −0.974 28.098 1.00 15.05 ATOM 1059 CA THR A 668 33.2110.308 28.428 1.00 16.29 ATOM 1060 CB THR A 668 32.670 1.432 27.520 1.0016.12 ATOM 1061 OG1 THR A 668 31.237 1.448 27.567 1.00 19.49 ATOM 1062CG2 THR A 668 33.133 1.207 26.078 1.00 15.93 ATOM 1063 C THR A 66832.995 0.672 29.895 1.00 18.10 ATOM 1064 O THR A 668 33.158 1.830 30.2971.00 20.65 ATOM 1065 N ASN A 669 32.617 −0.330 30.682 1.00 17.75 ATOM1066 CA ASN A 669 32.402 −0.177 32.115 1.00 20.15 ATOM 1067 CB ASN A 66933.749 0.053 32.797 1.00 28.92 ATOM 1068 CG ASN A 669 34.791 −0.95532.361 1.00 34.79 ATOM 1069 OD1 ASN A 669 34.619 −2.160 32.543 1.0040.75 ATOM 1070 ND2 ASN A 669 35.877 −0.468 31.772 1.00 36.76 ATOM 1071C ASN A 669 31.428 0.926 32.515 1.00 20.87 ATOM 1072 O ASN A 669 31.6901.696 33.443 1.00 21.59 ATOM 1073 N SER A 670 30.302 0.996 31.819 1.0017.34 ATOM 1074 CA SER A 670 29.286 1.992 32.120 1.00 19.60 ATOM 1075 CBSER A 670 28.103 1.836 31.160 1.00 18.96 ATOM 1076 OG SER A 670 27.0232.672 31.535 1.00 22.69 ATOM 1077 C SER A 670 28.803 1.787 33.551 1.0016.24 ATOM 1078 O SER A 670 28.755 0.655 34.041 1.00 14.46 ATOM 1079 NGLU A 671 28.455 2.879 34.227 1.00 18.45 ATOM 1080 CA GLU A 671 27.9512.775 35.589 1.00 19.69 ATOM 1081 CB GLU A 671 27.756 4.154 36.209 1.0017.48 ATOM 1082 CG GLU A 671 28.985 5.024 36.189 1.00 31.14 ATOM 1083 CDGLU A 671 28.901 6.156 37.191 1.00 32.78 ATOM 1084 OE1 GLU A 671 27.8306.796 37.291 1.00 31.62 ATOM 1085 OE2 GLU A 671 29.914 6.406 37.875 1.0026.52 ATOM 1086 C GLU A 671 26.611 2.058 35.549 1.00 18.77 ATOM 1087 OGLU A 671 26.253 1.332 36.482 1.00 19.75 ATOM 1088 N LEU A 672 25.8682.281 34.466 1.00 17.92 ATOM 1089 CA LEU A 672 24.569 1.646 34.279 1.0015.76 ATOM 1090 CB LEU A 672 23.954 2.067 32.942 1.00 12.50 ATOM 1091 CGLEU A 672 23.478 3.509 32.771 1.00 18.92 ATOM 1092 CD1 LEU A 672 23.1013.741 31.314 1.00 18.65 ATOM 1093 CD2 LEU A 672 22.292 3.766 33.678 1.0024.52 ATOM 1094 C LEU A 672 24.738 0.130 34.291 1.00 13.50 ATOM 1095 OLEU A 672 23.961 −0.586 34.912 1.00 12.92 ATOM 1096 N ALA A 673 25.755−0.358 33.590 1.00 13.11 ATOM 1097 CA ALA A 673 26.001 −1.792 33.5461.00 13.53 ATOM 1098 CB ALA A 673 27.169 −2.099 32.594 1.00 11.10 ATOM1099 C ALA A 673 26.318 −2.283 34.956 1.00 13.78 ATOM 1100 O ALA A 67325.925 −3.380 35.354 1.00 12.36 ATOM 1101 N LEU A 674 27.028 −1.45835.718 1.00 15.22 ATOM 1102 CA LEU A 674 27.394 −1.829 37.076 1.00 16.65ATOM 1103 CB LEU A 674 28.414 −0.832 37.632 1.00 18.96 ATOM 1104 CG LEUA 674 29.225 −1.323 38.832 1.00 26.52 ATOM 1105 CD1 LEU A 674 29.939−2.620 38.460 1.00 24.45 ATOM 1106 CD2 LEU A 674 30.231 −0.258 39.2461.00 20.57 ATOM 1107 C LEU A 674 26.152 −1.866 37.960 1.00 15.94 ATOM1108 O LEU A 674 25.930 −2.818 38.709 1.00 16.86 ATOM 1109 N MET A 67525.335 −0.822 37.851 1.00 19.35 ATOM 1110 CA MET A 675 24.107 −0.69438.627 1.00 18.57 ATOM 1111 CB MET A 675 23.413 0.641 38.312 1.00 29.02ATOM 1112 CG MET A 675 24.180 1.882 38.753 1.00 32.86 ATOM 1113 SD MET A675 23.766 3.373 37.785 1.00 38.23 ATOM 1114 CE MET A 675 22.129 3.76938.381 1.00 40.96 ATOM 1115 C MET A 675 23.133 −1.830 38.346 1.00 17.83ATOM 1116 O MET A 675 22.529 −2.383 39.265 1.00 17.84 ATOM 1117 N TYR A676 23.000 −2.184 37.073 1.00 15.75 ATOM 1118 CA TYR A 676 22.052 −3.21236.679 1.00 16.85 ATOM 1119 CB TYR A 676 21.293 −2.720 35.442 1.00 16.19ATOM 1120 CG TYR A 676 20.619 −1.374 35.668 1.00 20.30 ATOM 1121 CD1 TYRA 676 19.694 −1.197 36.691 1.00 31.51 ATOM 1122 CE1 TYR A 676 19.1070.045 36.922 1.00 18.89 ATOM 1123 CD2 TYR A 676 20.934 −0.276 34.8771.00 23.78 ATOM 1124 CE2 TYR A 676 20.354 0.962 35.097 1.00 27.90 ATOM1125 CZ TYR A 676 19.443 1.117 36.118 1.00 24.78 ATOM 1126 OH TYR A 67618.866 2.354 36.326 1.00 28.03 ATOM 1127 C TYR A 676 22.605 −4.62336.471 1.00 16.48 ATOM 1128 O TYR A 676 21.949 −5.478 35.872 1.00 15.88ATOM 1129 N ASN A 677 23.814 −4.863 36.968 1.00 16.14 ATOM 1130 CA ASN A677 24.433 −6.182 36.888 1.00 14.23 ATOM 1131 CB ASN A 677 23.666 −7.13837.812 1.00 21.33 ATOM 1132 CG ASN A 677 24.382 −8.452 38.022 1.00 29.37ATOM 1133 OD1 ASN A 677 25.570 −8.478 38.349 1.00 38.44 ATOM 1134 ND2ASN A 677 23.662 −9.555 37.847 1.00 42.62 ATOM 1135 C ASN A 677 24.516−6.765 35.474 1.00 15.05 ATOM 1136 O ASN A 677 24.332 −7.966 35.275 1.0014.59 ATOM 1137 N ASP A 678 24.802 −5.904 34.502 1.00 13.69 ATOM 1138 CAASP A 678 24.926 −6.302 33.100 1.00 16.08 ATOM 1139 CB ASP A 678 26.080−7.293 32.915 1.00 12.96 ATOM 1140 CG ASP A 678 27.430 −6.691 33.2341.00 18.27 ATOM 1141 OD1 ASP A 678 27.519 −5.452 33.377 1.00 16.21 ATOM1142 OD2 ASP A 678 28.406 −7.464 33.334 1.00 20.95 ATOM 1143 C ASP A 67823.667 −6.919 32.499 1.00 16.35 ATOM 1144 O ASP A 678 23.731 −7.50931.420 1.00 17.49 ATOM 1145 N GLU A 679 22.534 −6.790 33.184 1.00 14.03ATOM 1146 CA GLU A 679 21.278 −7.358 32.690 1.00 14.39 ATOM 1147 CB GLUA 679 20.567 −8.133 33.799 1.00 14.04 ATOM 1148 CG GLU A 679 21.314−9.351 34.300 1.00 22.79 ATOM 1149 CD GLU A 679 20.514 −10.128 35.3301.00 43.42 ATOM 1150 OE1 GLU A 679 19.464 −10.699 34.964 1.00 51.30 ATOM1151 OE2 GLU A 679 20.931 −10.162 36.507 1.00 41.34 ATOM 1152 C GLU A679 20.320 −6.301 32.151 1.00 12.89 ATOM 1153 O GLU A 679 19.873 −5.43032.895 1.00 13.61 ATOM 1154 N SER A 680 19.993 −6.401 30.863 1.00 10.87ATOM 1155 CA SER A 680 19.086 −5.456 30.209 1.00 12.50 ATOM 1156 CB SERA 680 17.627 −5.787 30.555 1.00 12.08 ATOM 1157 OG SER A 680 17.267−7.087 30.111 1.00 11.26 ATOM 1158 C SER A 680 19.409 −4.038 30.663 1.0011.78 ATOM 1159 O SER A 680 18.517 −3.280 31.045 1.00 12.76 ATOM 1160 NVAL A 681 20.693 −3.693 30.617 1.00 9.67 ATOM 1161 CA VAL A 681 21.183−2.386 31.049 1.00 7.19 ATOM 1162 CB VAL A 681 22.688 −2.248 30.725 1.0011.97 ATOM 1163 CG1 VAL A 681 23.219 −0.917 31.245 1.00 10.98 ATOM 1164CG2 VAL A 681 23.460 −3.423 31.346 1.00 12.93 ATOM 1165 C VAL A 68120.426 −1.195 30.453 1.00 9.58 ATOM 1166 O VAL A 681 19.870 −0.37831.185 1.00 10.02 ATOM 1167 N LEU A 681A 20.420 −1.094 29.128 1.00 9.51ATOM 1168 CA LEU A 681A 19.718 −0.011 28.443 1.00 10.16 ATOM 1169 CB LEUA 681A 19.773 −0.216 26.929 1.00 7.24 ATOM 1170 CG LEU A 681A 21.0790.035 26.178 1.00 9.74 ATOM 1171 CD1 LEU A 681A 20.979 −0.563 24.7881.00 13.02 ATOM 1172 CD2 LEU A 681A 21.345 1.526 26.102 1.00 15.84 ATOM1173 C LEU A 681A 18.253 0.049 28.851 1.00 8.34 ATOM 1174 O LEU A 681A17.725 1.118 29.174 1.00 10.62 ATOM 1175 N GLU A 682 17.599 −1.11028.834 1.00 10.08 ATOM 1176 CA GLU A 682 16.183 −1.191 29.161 1.00 7.57ATOM 1177 CB GLU A 682 15.667 −2.599 28.855 1.00 6.60 ATOM 1178 CG GLU A682 15.731 −2.954 27.348 1.00 8.78 ATOM 1179 CD GLU A 682 17.151 −3.19926.835 1.00 12.12 ATOM 1180 OE1 GLU A 682 18.001 −3.693 27.614 1.0010.38 ATOM 1181 OE2 GLU A 682 17.418 −2.919 25.646 1.00 10.27 ATOM 1182C GLU A 682 15.867 −0.773 30.594 1.00 8.81 ATOM 1183 O GLU A 682 14.829−0.158 30.854 1.00 7.94 ATOM 1184 N HIS A 683 16.752 −1.099 31.526 1.009.05 ATOM 1185 CA HIS A 683 16.531 −0.677 32.897 1.00 10.40 ATOM 1186 CBHIS A 683 17.561 −1.324 33.830 1.00 11.92 ATOM 1187 CG HIS A 683 17.161−2.686 34.296 1.00 10.38 ATOM 1188 CD2 HIS A 683 17.557 −3.920 33.9031.00 9.93 ATOM 1189 ND1 HIS A 683 16.172 −2.888 35.238 1.00 14.33 ATOM1190 CE1 HIS A 683 15.977 −4.183 35.400 1.00 7.54 ATOM 1191 NE2 HIS A683 16.806 −4.831 34.599 1.00 15.67 ATOM 1192 C HIS A 683 16.631 0.84632.925 1.00 11.08 ATOM 1193 O HIS A 683 15.868 1.512 33.621 1.00 10.48ATOM 1194 N HIS A 684 17.553 1.397 32.138 1.00 10.86 ATOM 1195 CA HIS A684 17.710 2.844 32.076 1.00 9.98 ATOM 1196 CB HIS A 684 18.941 3.23331.256 1.00 9.09 ATOM 1197 CG HIS A 684 19.229 4.697 31.284 1.00 8.54ATOM 1198 CD2 HIS A 684 19.399 5.555 32.322 1.00 5.20 ATOM 1199 ND1 HISA 684 19.313 5.467 30.142 1.00 17.15 ATOM 1200 CE1 HIS A 684 19.5186.728 30.474 1.00 9.30 ATOM 1201 NE2 HIS A 684 19.573 6.807 31.795 1.0015.79 ATOM 1202 C HIS A 684 16.473 3.502 31.465 1.00 9.44 ATOM 1203 OHIS A 684 16.020 4.542 31.941 1.00 11.75 ATOM 1204 N HIS A 685 15.9292.898 30.411 1.00 9.42 ATOM 1205 CA HIS A 685 14.740 3.447 29.757 1.007.57 ATOM 1206 CB HIS A 685 14.361 2.621 28.521 1.00 14.86 ATOM 1207 CGHIS A 685 15.472 2.468 27.521 1.00 7.24 ATOM 1208 CD2 HIS A 685 15.8461.402 26.773 1.00 9.32 ATOM 1209 ND1 HIS A 685 16.299 3.506 27.161 1.008.86 ATOM 1210 CE1 HIS A 685 17.141 3.088 26.227 1.00 14.03 ATOM 1211NE2 HIS A 685 16.886 1.819 25.974 1.00 8.62 ATOM 1212 C HIS A 685 13.5743.446 30.747 1.00 9.27 ATOM 1213 O HIS A 685 12.798 4.401 30.805 1.009.78 ATOM 1214 N PHE A 686 13.439 2.376 31.523 1.00 8.10 ATOM 1215 CAPHE A 686 12.351 2.314 32.507 1.00 10.05 ATOM 1216 CB PHE A 686 12.2910.923 33.151 1.00 8.82 ATOM 1217 CG PHE A 686 11.281 0.808 34.263 1.0010.55 ATOM 1218 CD1 PHE A 686 9.937 1.078 34.035 1.00 10.53 ATOM 1219CD2 PHE A 686 11.674 0.442 35.538 1.00 11.42 ATOM 1220 CE1 PHE A 6869.013 0.985 35.061 1.00 14.12 ATOM 1221 CE2 PHE A 686 10.754 0.34836.568 1.00 15.20 ATOM 1222 CZ PHE A 686 9.423 0.618 36.328 1.00 13.66ATOM 1223 C PHE A 686 12.554 3.391 33.570 1.00 9.59 ATOM 1224 O PHE A686 11.599 4.036 34.022 1.00 11.10 ATOM 1225 N ASP A 687 13.807 3.60333.965 1.00 10.38 ATOM 1226 CA ASP A 687 14.169 4.620 34.950 1.00 13.63ATOM 1227 CB ASP A 687 15.699 4.646 35.147 1.00 15.63 ATOM 1228 CG ASP A687 16.163 5.810 36.032 1.00 35.43 ATOM 1229 OD1 ASP A 687 15.842 5.81237.238 1.00 39.21 ATOM 1230 OD2 ASP A 687 16.855 6.721 35.514 1.00 46.67ATOM 1231 C ASP A 687 13.701 5.983 34.453 1.00 11.19 ATOM 1232 O ASP A687 13.079 6.742 35.191 1.00 12.63 ATOM 1233 N GLN A 688 14.026 6.26633.194 1.00 10.97 ATOM 1234 CA GLN A 688 13.664 7.531 32.571 1.00 10.87ATOM 1235 CB GLN A 688 14.331 7.623 31.193 1.00 15.23 ATOM 1236 CG GLN A688 15.844 7.876 31.260 1.00 11.96 ATOM 1237 CD GLN A 688 16.179 9.35031.456 1.00 14.39 ATOM 1238 OE1 GLN A 688 15.805 10.193 30.640 1.0020.66 ATOM 1239 NE2 GLN A 688 16.881 9.663 32.535 1.00 29.50 ATOM 1240 CGLN A 688 12.158 7.651 32.455 1.00 10.36 ATOM 1241 O GLN A 688 11.5878.729 32.641 1.00 10.53 ATOM 1242 N CYS A 689 11.495 6.536 32.160 1.008.48 ATOM 1243 CA CYS A 689 10.043 6.517 32.040 1.00 9.59 ATOM 1244 CBCYS A 689 9.558 5.097 31.706 1.00 11.54 ATOM 1245 SG CYS A 689 7.7724.940 31.573 1.00 11.98 ATOM 1246 C CYS A 689 9.406 7.005 33.343 1.0010.54 ATOM 1247 O CYS A 689 8.559 7.905 33.331 1.00 10.86 ATOM 1248 NLEU A 690 9.822 6.417 34.463 1.00 12.43 ATOM 1249 CA LEU A 690 9.3166.786 35.787 1.00 13.70 ATOM 1250 CB LEU A 690 9.968 5.912 36.863 1.0015.35 ATOM 1251 CG LEU A 690 9.620 4.423 36.853 1.00 18.35 ATOM 1252 CD1LEU A 690 10.326 3.723 38.008 1.00 25.25 ATOM 1253 CD2 LEU A 690 8.1184.248 36.969 1.00 17.06 ATOM 1254 C LEU A 690 9.605 8.247 36.093 1.0014.05 ATOM 1255 O LEU A 690 8.767 8.975 36.633 1.00 15.63 ATOM 1256 NMET A 691 10.817 8.681 35.750 1.00 13.87 ATOM 1257 CA MET A 691 11.25610.042 35.975 1.00 14.41 ATOM 1258 CB MET A 691 12.676 10.212 35.4111.00 14.62 ATOM 1259 CG MET A 691 13.371 11.496 35.757 1.00 32.36 ATOM1260 SD MET A 691 12.902 12.755 34.635 1.00 45.55 ATOM 1261 CE MET A 69113.918 12.471 33.200 1.00 37.72 ATOM 1262 C MET A 691 10.285 11.02435.336 1.00 13.72 ATOM 1263 O MET A 691 9.863 11.990 35.971 1.00 14.45ATOM 1264 N ILE A 692 9.903 10.758 34.091 1.00 10.48 ATOM 1265 CA ILE A692 8.980 11.644 33.400 1.00 9.98 ATOM 1266 CB ILE A 692 8.966 11.37131.895 1.00 10.00 ATOM 1267 CG2 ILE A 692 7.909 12.240 31.224 1.00 12.51ATOM 1268 CG1 ILE A 692 10.346 11.691 31.315 1.00 14.40 ATOM 1269 CD1ILE A 692 10.482 11.400 29.841 1.00 19.81 ATOM 1270 C ILE A 692 7.57811.534 33.973 1.00 10.09 ATOM 1271 O ILE A 692 6.906 12.547 34.166 1.0011.41 ATOM 1272 N LEU A 693 7.149 10.316 34.288 1.00 12.13 ATOM 1273 CALEU A 693 5.821 10.111 34.862 1.00 13.85 ATOM 1274 CB LEU A 693 5.5488.615 35.058 1.00 13.96 ATOM 1275 CG LEU A 693 5.212 7.826 33.789 1.0010.33 ATOM 1276 CD1 LEU A 693 5.183 6.335 34.082 1.00 17.28 ATOM 1277CD2 LEU A 693 3.868 8.305 33.243 1.00 9.40 ATOM 1278 C LEU A 693 5.64410.837 36.193 1.00 14.19 ATOM 1279 O LEU A 693 4.524 11.179 36.577 1.0016.64 ATOM 1280 N ASN A 694 6.747 11.073 36.893 1.00 16.46 ATOM 1281 CAASN A 694 6.697 11.755 38.183 1.00 16.63 ATOM 1282 CB ASN A 694 7.68611.116 39.159 1.00 20.12 ATOM 1283 CG ASN A 694 7.231 9.760 39.641 1.0024.99 ATOM 1284 OD1 ASN A 694 7.869 8.742 39.373 1.00 30.33 ATOM 1285ND2 ASN A 694 6.115 9.736 40.360 1.00 25.93 ATOM 1286 C ASN A 694 6.98913.247 38.101 1.00 18.31 ATOM 1287 O ASN A 694 6.855 13.958 39.093 1.0018.26 ATOM 1288 N SER A 695 7.395 13.721 36.930 1.00 16.05 ATOM 1289 CASER A 695 7.704 15.139 36.755 1.00 17.70 ATOM 1290 CB SER A 695 8.32115.376 35.376 1.00 19.30 ATOM 1291 OG SER A 695 9.607 14.793 35.298 1.0034.04 ATOM 1292 C SER A 695 6.471 16.022 36.914 1.00 15.83 ATOM 1293 OSER A 695 5.400 15.710 36.406 1.00 17.46 ATOM 1294 N PRO A 696 6.61117.144 37.630 1.00 18.97 ATOM 1295 CD PRO A 696 7.779 17.577 38.415 1.0026.97 ATOM 1296 CA PRO A 696 5.480 18.053 37.830 1.00 18.99 ATOM 1297 CBPRO A 696 6.113 19.220 38.579 1.00 22.14 ATOM 1298 CG PRO A 696 7.15418.534 39.414 1.00 28.71 ATOM 1299 C PRO A 696 4.866 18.480 36.498 1.0016.02 ATOM 1300 O PRO A 696 5.585 18.839 35.564 1.00 18.08 ATOM 1301 NGLY A 697 3.539 18.425 36.418 1.00 16.17 ATOM 1302 CA GLY A 697 2.84318.804 35.201 1.00 16.65 ATOM 1303 C GLY A 697 2.862 17.725 34.130 1.0014.72 ATOM 1304 O GLY A 697 2.283 17.901 33.060 1.00 15.86 ATOM 1305 NASN A 698 3.511 16.601 34.424 1.00 14.68 ATOM 1306 CA ASN A 698 3.62115.493 33.471 1.00 14.66 ATOM 1307 CB ASN A 698 5.099 15.209 33.174 1.0015.25 ATOM 1308 CG ASN A 698 5.760 16.304 32.365 1.00 19.94 ATOM 1309OD1 ASN A 698 5.883 16.199 31.146 1.00 13.89 ATOM 1310 ND2 ASN A 6986.186 17.367 33.039 1.00 16.33 ATOM 1311 C ASN A 698 2.990 14.198 33.9731.00 14.82 ATOM 1312 O ASN A 698 3.044 13.174 33.293 1.00 13.20 ATOM1313 N GLN A 699 2.379 14.243 35.151 1.00 13.46 ATOM 1314 CA GLN A 6991.807 13.041 35.749 1.00 14.53 ATOM 1315 CB GLN A 699 1.652 13.28137.251 1.00 16.25 ATOM 1316 CG GLN A 699 2.957 13.713 37.902 1.00 17.08ATOM 1317 CD GLN A 699 2.787 14.103 39.350 1.00 37.15 ATOM 1318 OE1 GLNA 699 2.147 15.105 39.661 1.00 41.13 ATOM 1319 NE2 GLN A 699 3.35713.307 40.248 1.00 41.91 ATOM 1320 C GLN A 699 0.499 12.522 35.158 1.0013.96 ATOM 1321 O GLN A 699 −0.567 12.676 35.754 1.00 15.67 ATOM 1322 NILE A 700 0.582 11.867 34.003 1.00 13.44 ATOM 1323 CA ILE A 700 −0.61711.348 33.356 1.00 14.25 ATOM 1324 CB ILE A 700 −0.345 10.974 31.8811.00 15.57 ATOM 1325 CG2 ILE A 700 0.010 12.222 31.086 1.00 15.78 ATOM1326 CG1 ILE A 700 0.777 9.941 31.793 1.00 16.74 ATOM 1327 CD1 ILE A 7000.940 9.361 30.407 1.00 12.98 ATOM 1328 C ILE A 700 −1.262 10.151 34.0641.00 13.88 ATOM 1329 O ILE A 700 −2.342 9.709 33.673 1.00 14.53 ATOM1330 N LEU A 701 −0.609 9.624 35.098 1.00 11.60 ATOM 1331 CA LEU A 701−1.169 8.495 35.845 1.00 14.58 ATOM 1332 CB LEU A 701 −0.150 7.35835.965 1.00 13.85 ATOM 1333 CG LEU A 701 0.310 6.673 34.677 1.00 11.07ATOM 1334 CD1 LEU A 701 1.270 5.539 35.031 1.00 13.34 ATOM 1335 CD2 LEUA 701 −0.895 6.128 33.921 1.00 12.89 ATOM 1336 C LEU A 701 −1.612 8.91437.247 1.00 13.75 ATOM 1337 O LEU A 701 −2.053 8.084 38.040 1.00 15.74ATOM 1338 N SER A 702 −1.497 10.201 37.547 1.00 15.74 ATOM 1339 CA SER A702 −1.872 10.717 38.860 1.00 18.36 ATOM 1340 CB SER A 702 −1.573 12.21738.949 1.00 20.19 ATOM 1341 OG SER A 702 −2.446 12.958 38.113 1.00 21.94ATOM 1342 C SER A 702 −3.347 10.490 39.176 1.00 19.34 ATOM 1343 O SER A702 −3.754 10.559 40.336 1.00 20.75 ATOM 1344 N GLY A 703 −4.144 10.22438.148 1.00 18.92 ATOM 1345 CA GLY A 703 −5.565 10.012 38.359 1.00 20.40ATOM 1346 C GLY A 703 −5.944 8.600 38.764 1.00 21.19 ATOM 1347 O GLY A703 −7.036 8.369 39.284 1.00 20.43 ATOM 1348 N LEU A 704 −5.045 7.64938.539 1.00 16.00 ATOM 1349 CA LEU A 704 −5.326 6.259 38.876 1.00 15.59ATOM 1350 CB LEU A 704 −4.262 5.335 38.278 1.00 9.29 ATOM 1351 CG LEU A704 −4.459 4.921 36.823 1.00 14.10 ATOM 1352 CD1 LEU A 704 −4.510 6.14335.926 1.00 17.73 ATOM 1353 CD2 LEU A 704 −3.312 3.998 36.418 1.00 11.19ATOM 1354 C LEU A 704 −5.419 5.993 40.368 1.00 16.40 ATOM 1355 O LEU A704 −4.773 6.659 41.178 1.00 16.88 ATOM 1356 N SER A 705 −6.233 5.00440.721 1.00 15.43 ATOM 1357 CA SER A 705 −6.395 4.621 42.111 1.00 15.96ATOM 1358 CB SER A 705 −7.556 3.640 42.268 1.00 15.57 ATOM 1359 OG SER A705 −7.242 2.402 41.658 1.00 15.44 ATOM 1360 C SER A 705 −5.092 3.94742.515 1.00 16.32 ATOM 1361 O SER A 705 −4.280 3.583 41.662 1.00 17.25ATOM 1362 N ILE A 706 −4.886 3.782 43.812 1.00 17.56 ATOM 1363 CA ILE A706 −3.666 3.164 44.292 1.00 16.88 ATOM 1364 CB ILE A 706 −3.679 3.08645.836 1.00 21.33 ATOM 1365 CG2 ILE A 706 −2.466 2.331 46.335 1.00 23.53ATOM 1366 CG1 ILE A 706 −3.712 4.507 46.411 1.00 21.96 ATOM 1367 CD1 ILEA 706 −3.892 4.577 47.918 1.00 22.24 ATOM 1368 C ILE A 706 −3.415 1.78243.685 1.00 16.48 ATOM 1369 O ILE A 706 −2.291 1.470 43.291 1.00 18.62ATOM 1370 N GLU A 707 −4.456 0.962 43.584 1.00 15.92 ATOM 1371 CA GLU A707 −4.304 −0.376 43.019 1.00 14.53 ATOM 1372 CB GLU A 707 −5.509 −1.25043.378 1.00 19.33 ATOM 1373 CG GLU A 707 −5.518 −1.682 44.836 1.00 24.82ATOM 1374 CD GLU A 707 −4.269 −2.460 45.214 1.00 31.26 ATOM 1375 OE1 GLUA 707 −4.029 −3.525 44.610 1.00 34.47 ATOM 1376 OE2 GLU A 707 −3.525−2.006 46.110 1.00 30.79 ATOM 1377 C GLU A 707 −4.093 −0.385 41.507 1.0014.27 ATOM 1378 O GLU A 707 −3.283 −1.156 41.002 1.00 15.02 ATOM 1379 NGLU A 708 −4.818 0.458 40.782 1.00 11.81 ATOM 1380 CA GLU A 708 −4.6440.495 39.337 1.00 12.49 ATOM 1381 CB GLU A 708 −5.756 1.317 38.673 1.0014.73 ATOM 1382 CG GLU A 708 −7.134 0.663 38.813 1.00 11.98 ATOM 1383 CDGLU A 708 −8.088 1.020 37.683 1.00 18.01 ATOM 1384 OE1 GLU A 708 −8.1212.196 37.274 1.00 19.76 ATOM 1385 OE2 GLU A 708 −8.816 0.120 37.216 1.0022.22 ATOM 1386 C GLU A 708 −3.264 1.054 38.996 1.00 14.00 ATOM 1387 OGLU A 708 −2.624 0.607 38.047 1.00 12.79 ATOM 1388 N TYR A 709 −2.7982.018 39.784 1.00 12.70 ATOM 1389 CA TYR A 709 −1.482 2.604 39.551 1.0013.42 ATOM 1390 CB TYR A 709 −1.204 3.724 40.557 1.00 12.05 ATOM 1391 CGTYR A 709 0.129 4.407 40.339 1.00 19.13 ATOM 1392 CD1 TYR A 709 0.3115.302 39.296 1.00 14.81 ATOM 1393 CE1 TYR A 709 1.530 5.928 39.091 1.0015.81 ATOM 1394 CD2 TYR A 709 1.207 4.149 41.174 1.00 17.39 ATOM 1395CE2 TYR A 709 2.427 4.767 40.978 1.00 18.97 ATOM 1396 CZ TYR A 709 2.5835.658 39.934 1.00 17.67 ATOM 1397 OH TYR A 709 3.793 6.284 39.737 1.0018.77 ATOM 1398 C TYR A 709 −0.424 1.515 39.708 1.00 15.44 ATOM 1399 OTYR A 709 0.452 1.348 38.855 1.00 15.06 ATOM 1400 N LYS A 710 −0.5200.774 40.808 1.00 15.25 ATOM 1401 CA LYS A 710 0.409 −0.311 41.095 1.0015.31 ATOM 1402 CB LYS A 710 −0.020 −1.026 42.379 1.00 22.10 ATOM 1403CG LYS A 710 0.809 −2.249 42.716 1.00 23.74 ATOM 1404 CD LYS A 710 0.299−2.931 43.978 1.00 33.24 ATOM 1405 CE LYS A 710 0.996 −4.263 44.204 1.0039.08 ATOM 1406 NZ LYS A 710 2.478 −4.117 44.248 1.00 42.37 ATOM 1407 CLYS A 710 0.474 −1.309 39.939 1.00 14.94 ATOM 1408 O LYS A 710 1.555−1.645 39.448 1.00 12.87 ATOM 1409 N THR A 711 −0.692 −1.777 39.506 1.0013.50 ATOM 1410 CA THR A 711 −0.783 −2.736 38.411 1.00 12.45 ATOM 1411CB THR A 711 −2.249 −3.092 38.128 1.00 17.44 ATOM 1412 OG1 THR A 711−2.791 −3.792 39.255 1.00 21.96 ATOM 1413 CG2 THR A 711 −2.365 −3.95336.872 1.00 16.75 ATOM 1414 C THR A 711 −0.161 −2.198 37.129 1.00 11.72ATOM 1415 O THR A 711 0.597 −2.896 36.442 1.00 13.19 ATOM 1416 N THR A712 −0.487 −0.954 36.809 1.00 11.15 ATOM 1417 CA THR A 712 0.015 −0.31935.599 1.00 13.99 ATOM 1418 CB THR A 712 −0.598 1.081 35.424 1.00 9.97ATOM 1419 OG1 THR A 712 −2.029 0.967 35.357 1.00 14.40 ATOM 1420 CG2 THRA 712 −0.088 1.729 34.133 1.00 12.92 ATOM 1421 C THR A 712 1.541 −0.22135.556 1.00 12.77 ATOM 1422 O THR A 712 2.158 −0.596 34.559 1.00 12.54ATOM 1423 N LEU A 713 2.156 0.275 36.625 1.00 12.50 ATOM 1424 CA LEU A713 3.612 0.384 36.638 1.00 11.02 ATOM 1425 CB LEU A 713 4.105 1.02337.940 1.00 13.58 ATOM 1426 CG LEU A 713 3.889 2.528 38.100 1.00 22.03ATOM 1427 CD1 LEU A 713 4.754 3.042 39.250 1.00 21.64 ATOM 1428 CD2 LEUA 713 4.261 3.241 36.809 1.00 27.88 ATOM 1429 C LEU A 713 4.298 −0.96736.438 1.00 13.04 ATOM 1430 O LEU A 713 5.340 −1.048 35.785 1.00 12.26ATOM 1431 N LYS A 714 3.718 −2.026 36.995 1.00 11.66 ATOM 1432 CA LYS A714 4.304 −3.356 36.852 1.00 12.24 ATOM 1433 CB LYS A 714 3.540 −4.38337.690 1.00 17.46 ATOM 1434 CG LYS A 714 3.582 −4.123 39.182 1.00 27.51ATOM 1435 CD LYS A 714 2.878 −5.236 39.939 1.00 33.99 ATOM 1436 CE LYS A714 2.899 −4.988 41.433 1.00 42.93 ATOM 1437 NZ LYS A 714 2.222 −6.09242.168 1.00 46.33 ATOM 1438 C LYS A 714 4.284 −3.784 35.390 1.00 12.70ATOM 1439 O LYS A 714 5.259 −4.338 34.886 1.00 12.91 ATOM 1440 N ILE A715 3.168 −3.525 34.717 1.00 10.95 ATOM 1441 CA ILE A 715 3.023 −3.86933.308 1.00 10.57 ATOM 1442 CB ILE A 715 1.586 −3.590 32.820 1.00 11.39ATOM 1443 CG2 ILE A 715 1.468 −3.896 31.339 1.00 11.35 ATOM 1444 CG1 ILEA 715 0.596 −4.450 33.613 1.00 12.69 ATOM 1445 CD1 ILE A 715 −0.854−4.130 33.332 1.00 13.44 ATOM 1446 C ILE A 715 4.017 −3.052 32.482 1.0010.34 ATOM 1447 O ILE A 715 4.676 −3.581 31.588 1.00 11.86 ATOM 1448 NILE A 716 4.133 −1.762 32.793 1.00 10.78 ATOM 1449 CA ILE A 716 5.069−0.886 32.081 1.00 9.90 ATOM 1450 CB ILE A 716 4.989 0.563 32.621 1.0010.08 ATOM 1451 CG2 ILE A 716 6.171 1.387 32.115 1.00 10.86 ATOM 1452CG1 ILE A 716 3.661 1.197 32.189 1.00 10.91 ATOM 1453 CD1 ILE A 7163.413 2.564 32.792 1.00 11.27 ATOM 1454 C ILE A 716 6.508 −1.393 32.1961.00 8.77 ATOM 1455 O ILE A 716 7.229 −1.487 31.199 1.00 9.34 ATOM 1456N LYS A 717 6.926 −1.724 33.413 1.00 9.18 ATOM 1457 CA LYS A 717 8.275−2.235 33.623 1.00 10.88 ATOM 1458 CB LYS A 717 8.489 −2.606 35.087 1.0012.47 ATOM 1459 CG LYS A 717 9.790 −3.366 35.337 1.00 14.78 ATOM 1460 CDLYS A 717 9.865 −3.864 36.775 1.00 17.70 ATOM 1461 CE LYS A 717 11.045−4.809 36.977 1.00 29.85 ATOM 1462 NZ LYS A 717 11.082 −5.374 38.3551.00 25.71 ATOM 1463 C LYS A 717 8.540 −3.469 32.752 1.00 10.54 ATOM1464 O LYS A 717 9.536 −3.524 32.041 1.00 10.05 ATOM 1465 N GLN A 7187.647 −4.451 32.847 1.00 11.40 ATOM 1466 CA GLN A 718 7.774 −5.68232.067 1.00 11.80 ATOM 1467 CB GLN A 718 6.635 −6.628 32.434 1.00 11.33ATOM 1468 CG GLN A 718 6.683 −6.965 33.899 1.00 14.75 ATOM 1469 CD GLN A718 7.954 −7.691 34.293 1.00 35.80 ATOM 1470 OE1 GLN A 718 8.774 −7.17635.053 1.00 49.66 ATOM 1471 NE2 GLN A 718 8.115 −8.909 33.784 1.00 43.62ATOM 1472 C GLN A 718 7.778 −5.422 30.559 1.00 9.82 ATOM 1473 O GLN A718 8.559 −6.027 29.831 1.00 9.86 ATOM 1474 N ALA A 719 6.920 −4.51830.108 1.00 8.83 ATOM 1475 CA ALA A 719 6.842 −4.205 28.686 1.00 10.49ATOM 1476 CB ALA A 719 5.657 −3.292 28.436 1.00 5.96 ATOM 1477 C ALA A719 8.129 −3.560 28.186 1.00 9.98 ATOM 1478 O ALA A 719 8.618 −3.89227.101 1.00 9.19 ATOM 1479 N ILE A 720 8.688 −2.641 28.971 1.00 7.25ATOM 1480 CA ILE A 720 9.920 −1.988 28.548 1.00 8.66 ATOM 1481 CB ILE A720 10.233 −0.753 29.426 1.00 10.86 ATOM 1482 CG2 ILE A 720 11.616−0.193 29.086 1.00 11.64 ATOM 1483 CG1 ILE A 720 9.164 0.320 29.181 1.0011.59 ATOM 1484 CD1 ILE A 720 9.367 1.605 29.976 1.00 12.21 ATOM 1485 CILE A 720 11.085 −2.974 28.580 1.00 10.02 ATOM 1486 O ILE A 720 11.883−3.040 27.641 1.00 8.95 ATOM 1487 N LEU A 721 11.178 −3.762 29.643 1.008.10 ATOM 1488 CA LEU A 721 12.264 −4.733 29.719 1.00 8.45 ATOM 1489 CBLEU A 721 12.251 −5.446 31.077 1.00 10.55 ATOM 1490 CG LEU A 721 12.613−4.553 32.267 1.00 13.26 ATOM 1491 CD1 LEU A 721 12.539 −5.350 33.5741.00 15.78 ATOM 1492 CD2 LEU A 721 14.006 −3.991 32.059 1.00 24.08 ATOM1493 C LEU A 721 12.173 −5.750 28.576 1.00 9.96 ATOM 1494 O LEU A 72113.195 −6.196 28.049 1.00 8.91 ATOM 1495 N ALA A 722 10.948 −6.08228.175 1.00 8.77 ATOM 1496 CA ALA A 722 10.715 −7.047 27.100 1.00 8.74ATOM 1497 CB ALA A 722 9.219 −7.218 26.879 1.00 9.06 ATOM 1498 C ALA A722 11.383 −6.648 25.786 1.00 10.10 ATOM 1499 O ALA A 722 11.704 −7.50724.965 1.00 13.26 ATOM 1500 N THR A 723 11.598 −5.350 25.585 1.00 8.97ATOM 1501 CA THR A 723 12.213 −4.884 24.344 1.00 10.94 ATOM 1502 CB THRA 723 11.943 −3.374 24.127 1.00 8.53 ATOM 1503 OG1 THR A 723 12.542−2.615 25.181 1.00 8.41 ATOM 1504 CG2 THR A 723 10.437 −3.114 24.1181.00 8.22 ATOM 1505 C THR A 723 13.713 −5.187 24.203 1.00 9.21 ATOM 1506O THR A 723 14.327 −4.862 23.186 1.00 12.03 ATOM 1507 N ASP A 724 14.308−5.797 25.223 1.00 9.75 ATOM 1508 CA ASP A 724 15.710 −6.203 25.133 1.007.82 ATOM 1509 CB ASP A 724 16.257 −6.533 26.525 1.00 12.18 ATOM 1510 CGASP A 724 17.648 −7.147 26.490 1.00 8.16 ATOM 1511 OD1 ASP A 724 18.232−7.299 25.394 1.00 11.70 ATOM 1512 OD2 ASP A 724 18.161 −7.481 27.5811.00 11.61 ATOM 1513 C ASP A 724 15.600 −7.475 24.293 1.00 8.26 ATOM1514 O ASP A 724 15.022 −8.459 24.742 1.00 10.28 ATOM 1515 N LEU A 72516.127 −7.452 23.073 1.00 9.50 ATOM 1516 CA LEU A 725 16.037 −8.61122.189 1.00 8.83 ATOM 1517 CB LEU A 725 16.791 −8.343 20.883 1.00 11.33ATOM 1518 CG LEU A 725 16.365 −9.236 19.717 1.00 16.17 ATOM 1519 CD1 LEUA 725 14.910 −8.953 19.367 1.00 12.02 ATOM 1520 CD2 LEU A 725 17.262−8.974 18.516 1.00 20.09 ATOM 1521 C LEU A 725 16.573 −9.880 22.849 1.0012.30 ATOM 1522 O LEU A 725 16.179 −10.994 22.498 1.00 11.52 ATOM 1523 NALA A 726 17.476 −9.712 23.806 1.00 11.08 ATOM 1524 CA ALA A 726 18.028−10.855 24.517 1.00 12.63 ATOM 1525 CB ALA A 726 19.104 −10.394 25.4891.00 21.41 ATOM 1526 C ALA A 726 16.918 −11.583 25.274 1.00 12.40 ATOM1527 O ALA A 726 16.914 −12.813 25.354 1.00 13.56 ATOM 1528 N LEU A 72715.985 −10.823 25.843 1.00 12.79 ATOM 1529 CA LEU A 727 14.884 −11.42126.591 1.00 14.99 ATOM 1530 CB LEU A 727 14.206 −10.380 27.485 1.0011.71 ATOM 1531 CG LEU A 727 15.096 −9.856 28.612 1.00 16.19 ATOM 1532CD1 LEU A 727 14.302 −8.925 29.511 1.00 13.74 ATOM 1533 CD2 LEU A 72715.631 −11.036 29.409 1.00 19.43 ATOM 1534 C LEU A 727 13.868 −12.04525.646 1.00 15.02 ATOM 1535 O LEU A 727 13.173 −12.996 26.005 1.00 15.57ATOM 1536 N TYR A 728 13.777 −11.500 24.438 1.00 12.38 ATOM 1537 CA TYRA 728 12.862 −12.038 23.435 1.00 12.71 ATOM 1538 CB TYR A 728 12.844−11.136 22.194 1.00 10.64 ATOM 1539 CG TYR A 728 12.303 −11.823 20.9601.00 12.57 ATOM 1540 CD1 TYR A 728 10.966 −12.197 20.875 1.00 14.71 ATOM1541 CE1 TYR A 728 10.473 −12.854 19.752 1.00 12.42 ATOM 1542 CD2 TYR A728 13.139 −12.124 19.888 1.00 13.44 ATOM 1543 CE2 TYR A 728 12.659−12.777 18.763 1.00 13.13 ATOM 1544 CZ TYR A 728 11.329 −13.142 18.6991.00 15.27 ATOM 1545 OH TYR A 728 10.857 −13.801 17.580 1.00 18.62 ATOM1546 C TYR A 728 13.350 −13.430 23.041 1.00 12.62 ATOM 1547 O TYR A 72812.588 −14.401 23.028 1.00 14.23 ATOM 1548 N ILE A 729 14.636 −13.52222.723 1.00 12.98 ATOM 1549 CA ILE A 729 15.232 −14.788 22.327 1.0013.19 ATOM 1550 CB ILE A 729 16.723 −14.595 21.983 1.00 14.56 ATOM 1551CG2 ILE A 729 17.395 −15.942 21.797 1.00 19.39 ATOM 1552 CG1 ILE A 72916.849 −13.727 20.727 1.00 18.02 ATOM 1553 CD1 ILE A 729 18.268 −13.30920.406 1.00 26.38 ATOM 1554 C ILE A 729 15.088 −15.826 23.439 1.00 15.70ATOM 1555 O ILE A 729 14.830 −17.001 23.178 1.00 14.36 ATOM 1556 N LYS A730 15.227 −15.375 24.681 1.00 15.21 ATOM 1557 CA LYS A 730 15.127−16.257 25.837 1.00 16.44 ATOM 1558 CB LYS A 730 15.657 −15.528 27.0751.00 21.43 ATOM 1559 CG LYS A 730 15.494 −16.291 28.376 1.00 27.38 ATOM1560 CD LYS A 730 16.133 −15.528 29.523 1.00 31.22 ATOM 1561 CE LYS A730 15.975 −16.267 30.839 1.00 36.43 ATOM 1562 NZ LYS A 730 16.672−15.556 31.947 1.00 41.27 ATOM 1563 C LYS A 730 13.727 −16.802 26.1331.00 16.48 ATOM 1564 O LYS A 730 13.573 −17.972 26.498 1.00 17.06 ATOM1565 N ARG A 731 12.707 −15.969 25.968 1.00 14.55 ATOM 1566 CA ARG A 73111.347 −16.395 26.283 1.00 15.57 ATOM 1567 CB ARG A 731 10.622 −15.29127.060 1.00 19.59 ATOM 1568 CG ARG A 731 11.309 −14.842 28.335 1.0018.25 ATOM 1569 CD ARG A 731 10.437 −13.846 29.086 1.00 33.93 ATOM 1570NE ARG A 731 9.209 −14.462 29.588 1.00 32.78 ATOM 1571 CZ ARG A 7318.168 −13.781 30.058 1.00 29.98 ATOM 1572 NH1 ARG A 731 8.197 −12.45630.091 1.00 30.21 ATOM 1573 NH2 ARG A 731 7.097 −14.426 30.501 1.0036.09 ATOM 1574 C ARG A 731 10.461 −16.807 25.118 1.00 12.75 ATOM 1575 OARG A 731 9.436 −17.454 25.325 1.00 15.30 ATOM 1576 N ARG A 732 10.841−16.445 23.897 1.00 13.21 ATOM 1577 CA ARG A 732 10.002 −16.759 22.7511.00 11.06 ATOM 1578 CB ARG A 732 10.589 −16.162 21.474 1.00 10.97 ATOM1579 CG ARG A 732 11.872 −16.812 21.021 1.00 12.09 ATOM 1580 CD ARG A732 12.325 −16.192 19.724 1.00 12.79 ATOM 1581 NE ARG A 732 13.525−16.822 19.193 1.00 13.80 ATOM 1582 CZ ARG A 732 13.919 −16.704 17.9301.00 20.20 ATOM 1583 NH1 ARG A 732 13.201 −15.980 17.077 1.00 23.11 ATOM1584 NH2 ARG A 732 15.025 −17.307 17.518 1.00 22.17 ATOM 1585 C ARG A732 9.751 −18.245 22.549 1.00 11.37 ATOM 1586 O ARG A 732 8.704 −18.62522.031 1.00 11.95 ATOM 1587 N GLY A 733 10.703 −19.078 22.962 1.00 13.25ATOM 1588 CA GLY A 733 10.543 −20.512 22.804 1.00 13.40 ATOM 1589 C GLYA 733 9.298 −21.009 23.508 1.00 14.10 ATOM 1590 O GLY A 733 8.543−21.823 22.970 1.00 15.18 ATOM 1591 N GLU A 734 9.080 −20.512 24.7191.00 11.89 ATOM 1592 CA GLU A 734 7.919 −20.900 25.505 1.00 14.43 ATOM1593 CB GLU A 734 7.988 −20.264 26.895 1.00 14.05 ATOM 1594 CG GLU A 7346.675 −20.312 27.661 1.00 18.08 ATOM 1595 CD GLU A 734 6.810 −19.82829.091 1.00 21.97 ATOM 1596 OE1 GLU A 734 7.742 −19.048 29.372 1.0019.31 ATOM 1597 OE2 GLU A 734 5.977 −20.221 29.932 1.00 32.96 ATOM 1598C GLU A 734 6.632 −20.478 24.806 1.00 14.65 ATOM 1599 O GLU A 734 5.663−21.235 24.760 1.00 14.67 ATOM 1600 N PHE A 735 6.631 −19.264 24.2671.00 15.01 ATOM 1601 CA PHE A 735 5.470 −18.729 23.566 1.00 11.90 ATOM1602 CB PHE A 735 5.743 −17.278 23.157 1.00 11.17 ATOM 1603 CG PHE A 7354.632 −16.635 22.366 1.00 16.06 ATOM 1604 CD1 PHE A 735 3.354 −16.51522.892 1.00 16.32 ATOM 1605 CD2 PHE A 735 4.885 −16.102 21.111 1.0013.68 ATOM 1606 CE1 PHE A 735 2.355 −15.869 22.178 1.00 13.80 ATOM 1607CE2 PHE A 735 3.897 −15.458 20.400 1.00 12.16 ATOM 1608 CZ PHE A 7352.631 −15.340 20.931 1.00 14.03 ATOM 1609 C PHE A 735 5.142 −19.56622.329 1.00 13.78 ATOM 1610 O PHE A 735 3.989 −19.946 22.117 1.00 13.01ATOM 1611 N PHE A 736 6.156 −19.853 21.517 1.00 12.56 ATOM 1612 CA PHE A736 5.952 −20.632 20.299 1.00 14.09 ATOM 1613 CB PHE A 736 7.242 −20.69119.472 1.00 15.66 ATOM 1614 CG PHE A 736 7.752 −19.342 19.031 1.00 17.77ATOM 1615 CD1 PHE A 736 6.888 −18.268 18.894 1.00 16.30 ATOM 1616 CD2PHE A 736 9.092 −19.166 18.701 1.00 14.18 ATOM 1617 CE1 PHE A 736 7.345−17.040 18.435 1.00 13.31 ATOM 1618 CE2 PHE A 736 9.558 −17.939 18.2421.00 13.12 ATOM 1619 CZ PHE A 736 8.686 −16.877 18.106 1.00 17.60 ATOM1620 C PHE A 736 5.483 −22.054 20.598 1.00 14.02 ATOM 1621 O PHE A 7364.653 −22.608 19.874 1.00 15.27 ATOM 1622 N GLU A 737 6.022 −22.64021.661 1.00 15.53 ATOM 1623 CA GLU A 737 5.667 −24.000 22.047 1.00 16.49ATOM 1624 CB GLU A 737 6.598 −24.493 23.155 1.00 18.16 ATOM 1625 CG GLUA 737 6.296 −25.908 23.623 1.00 32.20 ATOM 1626 CD GLU A 737 7.266−26.397 24.685 1.00 44.41 ATOM 1627 OE1 GLU A 737 7.368 −25.748 25.7481.00 43.95 ATOM 1628 OE2 GLU A 737 7.926 −27.433 24.457 1.00 45.00 ATOM1629 C GLU A 737 4.219 −24.105 22.505 1.00 16.86 ATOM 1630 O GLU A 7373.517 −25.050 22.137 1.00 18.64 ATOM 1631 N LEU A 738 3.774 −23.14423.308 1.00 15.93 ATOM 1632 CA LEU A 738 2.396 −23.140 23.791 1.00 14.96ATOM 1633 CB LEU A 738 2.137 −21.910 24.665 1.00 13.51 ATOM 1634 CG LEUA 738 2.817 −21.890 26.037 1.00 13.44 ATOM 1635 CD1 LEU A 738 2.813−20.474 26.589 1.00 14.08 ATOM 1636 CD2 LEU A 738 2.103 −22.844 26.9871.00 21.77 ATOM 1637 C LEU A 738 1.435 −23.137 22.610 1.00 15.65 ATOM1638 O LEU A 738 0.431 −23.854 22.610 1.00 17.64 ATOM 1639 N ILE A 7391.743 −22.323 21.604 1.00 13.75 ATOM 1640 CA ILE A 739 0.904 −22.23620.415 1.00 14.28 ATOM 1641 CB ILE A 739 1.388 −21.112 19.464 1.00 12.79ATOM 1642 CG2 ILE A 739 0.686 −21.224 18.118 1.00 23.84 ATOM 1643 CG1ILE A 739 1.122 −19.744 20.096 1.00 16.58 ATOM 1644 CD1 ILE A 739 1.656−18.576 19.279 1.00 13.81 ATOM 1645 C ILE A 739 0.925 −23.557 19.6541.00 16.17 ATOM 1646 O ILE A 739 −0.126 −24.107 19.309 1.00 18.24 ATOM1647 N ARG A 740 2.124 −24.075 19.410 1.00 15.35 ATOM 1648 CA ARG A 7402.274 −25.322 18.671 1.00 18.48 ATOM 1649 CB ARG A 740 3.758 −25.64818.474 1.00 23.15 ATOM 1650 CG ARG A 740 3.996 −26.804 17.508 1.00 35.46ATOM 1651 CD ARG A 740 5.475 −27.059 17.224 1.00 39.66 ATOM 1652 NE ARGA 740 6.174 −27.694 18.340 1.00 40.53 ATOM 1653 CZ ARG A 740 6.703−27.043 19.371 1.00 42.20 ATOM 1654 NH1 ARG A 740 6.623 −25.721 19.4411.00 52.88 ATOM 1655 NH2 ARG A 740 7.317 −27.718 20.335 1.00 44.19 ATOM1656 C ARG A 740 1.582 −26.495 19.360 1.00 19.41 ATOM 1657 O ARG A 7401.093 −27.410 18.698 1.00 18.06 ATOM 1658 N LYS A 741 1.539 −26.47020.686 1.00 18.03 ATOM 1659 CA LYS A 741 0.906 −27.553 21.430 1.00 18.11ATOM 1660 CB LYS A 741 1.696 −27.853 22.699 1.00 14.50 ATOM 1661 CG LYSA 741 3.074 −28.426 22.451 1.00 21.67 ATOM 1662 CD LYS A 741 3.717−28.812 23.763 1.00 23.36 ATOM 1663 CE LYS A 741 5.087 −29.430 23.5581.00 27.38 ATOM 1664 NZ LYS A 741 5.715 −29.747 24.871 1.00 23.91 ATOM1665 C LYS A 741 −0.540 −27.248 21.798 1.00 17.80 ATOM 1666 O LYS A 741−1.134 −27.940 22.623 1.00 18.63 ATOM 1667 N ASN A 742 −1.102 −26.21421.183 1.00 17.40 ATOM 1668 CA ASN A 742 −2.478 −25.822 21.456 1.0017.84 ATOM 1669 CB ASN A 742 −3.443 −26.841 20.849 1.00 16.88 ATOM 1670CG ASN A 742 −3.442 −26.801 19.335 1.00 15.02 ATOM 1671 OD1 ASN A 742−3.741 −25.772 18.733 1.00 28.97 ATOM 1672 ND2 ASN A 742 −3.100 −27.92318.709 1.00 20.44 ATOM 1673 C ASN A 742 −2.734 −25.671 22.949 1.00 17.96ATOM 1674 O ASN A 742 −3.727 −26.174 23.486 1.00 17.06 ATOM 1675 N GLN A743 −1.827 −24.964 23.615 1.00 16.68 ATOM 1676 CA GLN A 743 −1.937−24.727 25.045 1.00 17.92 ATOM 1677 CB GLN A 743 −0.738 −25.338 25.7771.00 20.38 ATOM 1678 CG GLN A 743 −0.461 −26.787 25.408 1.00 28.60 ATOM1679 CD GLN A 743 0.746 −27.350 26.131 1.00 30.94 ATOM 1680 OE1 GLN A743 1.775 −26.682 26.255 1.00 32.52 ATOM 1681 NE2 GLN A 743 0.634−28.588 26.602 1.00 20.21 ATOM 1682 C GLN A 743 −2.002 −23.233 25.3411.00 16.35 ATOM 1683 O GLN A 743 −2.175 −22.836 26.490 1.00 18.44 ATOM1684 N PHE A 744 −1.877 −22.407 24.307 1.00 16.26 ATOM 1685 CA PHE A 744−1.916 −20.959 24.501 1.00 19.79 ATOM 1686 CB PHE A 744 −1.627 −20.22923.184 1.00 21.58 ATOM 1687 CG PHE A 744 −1.465 −18.740 23.340 1.0017.97 ATOM 1688 CD1 PHE A 744 −0.441 −18.216 24.117 1.00 20.04 ATOM 1689CD2 PHE A 744 −2.345 −17.865 22.720 1.00 24.29 ATOM 1690 CE1 PHE A 744−0.298 −16.847 24.271 1.00 24.80 ATOM 1691 CE2 PHE A 744 −2.208 −16.49922.869 1.00 20.38 ATOM 1692 CZ PHE A 744 −1.184 −15.988 23.647 1.0026.24 ATOM 1693 C PHE A 744 −3.265 −20.515 25.060 1.00 19.74 ATOM 1694 OPHE A 744 −4.316 −20.860 24.526 1.00 21.03 ATOM 1695 N ASN A 745 −3.221−19.746 26.142 1.00 19.11 ATOM 1696 CA ASN A 745 −4.427 −19.260 26.7911.00 18.83 ATOM 1697 CB ASN A 745 −4.893 −20.270 27.839 1.00 14.11 ATOM1698 CG ASN A 745 −6.067 −19.764 28.653 1.00 17.45 ATOM 1699 OD1 ASN A745 −6.924 −19.042 28.143 1.00 22.19 ATOM 1700 ND2 ASN A 745 −6.120−20.152 29.921 1.00 30.84 ATOM 1701 C ASN A 745 −4.183 −17.906 27.4461.00 17.46 ATOM 1702 O ASN A 745 −3.518 −17.818 28.481 1.00 17.84 ATOM1703 N LEU A 746 −4.720 −16.857 26.826 1.00 16.56 ATOM 1704 CA LEU A 746−4.573 −15.497 27.323 1.00 18.48 ATOM 1705 CB LEU A 746 −5.163 −14.49526.323 1.00 15.11 ATOM 1706 CG LEU A 746 −4.319 −14.192 25.082 1.0017.98 ATOM 1707 CD1 LEU A 746 −5.031 −13.165 24.217 1.00 16.50 ATOM 1708CD2 LEU A 746 −2.960 −13.664 25.507 1.00 17.71 ATOM 1709 C LEU A 746−5.212 −15.284 28.688 1.00 21.08 ATOM 1710 O LEU A 746 −4.911 −14.30429.366 1.00 20.60 ATOM 1711 N GLU A 747 −6.098 −16.192 29.089 1.00 21.14ATOM 1712 CA GLU A 747 −6.748 −16.075 30.389 1.00 21.90 ATOM 1713 CB GLUA 747 −7.916 −17.058 30.504 1.00 20.33 ATOM 1714 CG GLU A 747 −9.179−16.586 29.813 1.00 31.82 ATOM 1715 CD GLU A 747 −10.324 −17.569 29.9591.00 40.12 ATOM 1716 OE1 GLU A 747 −10.550 −18.057 31.086 1.00 43.30ATOM 1717 OE2 GLU A 747 −11.003 −17.846 28.949 1.00 40.94 ATOM 1718 CGLU A 747 −5.740 −16.331 31.498 1.00 22.98 ATOM 1719 O GLU A 747 −5.885−15.826 32.612 1.00 23.46 ATOM 1720 N ASP A 748 −4.719 −17.124 31.1881.00 21.44 ATOM 1721 CA ASP A 748 −3.670 −17.424 32.151 1.00 21.15 ATOM1722 CB ASP A 748 −2.800 −18.579 31.651 1.00 19.25 ATOM 1723 CG ASP A748 −1.656 −18.899 32.595 1.00 19.90 ATOM 1724 OD1 ASP A 748 −0.710−18.088 32.692 1.00 26.86 ATOM 1725 OD2 ASP A 748 −1.704 −19.962 33.2461.00 42.46 ATOM 1726 C ASP A 748 −2.819 −16.171 32.314 1.00 20.94 ATOM1727 O ASP A 748 −2.240 −15.677 31.351 1.00 19.01 ATOM 1728 N PRO A 749−2.742 −15.637 33.541 1.00 18.53 ATOM 1729 CD PRO A 749 −3.443 −16.10834.750 1.00 26.08 ATOM 1730 CA PRO A 749 −1.958 −14.432 33.825 1.0019.83 ATOM 1731 CB PRO A 749 −2.009 −14.346 35.347 1.00 25.90 ATOM 1732CG PRO A 749 −3.377 −14.896 35.654 1.00 25.60 ATOM 1733 C PRO A 749−0.528 −14.476 33.286 1.00 17.96 ATOM 1734 O PRO A 749 −0.047 −13.50632.708 1.00 18.09 ATOM 1735 N HIS A 750 0.149 −15.603 33.475 1.00 17.27ATOM 1736 CA HIS A 750 1.520 −15.737 32.998 1.00 16.70 ATOM 1737 CB HISA 750 2.138 −17.039 33.509 1.00 14.57 ATOM 1738 CG HIS A 750 3.506−17.301 32.975 1.00 13.17 ATOM 1739 CD2 HIS A 750 4.710 −16.780 33.2991.00 15.22 ATOM 1740 ND1 HIS A 750 3.748 −18.181 31.933 1.00 20.55 ATOM1741 CE1 HIS A 750 5.030 −18.183 31.649 1.00 21.44 ATOM 1742 NE2 HIS A750 5.644 −17.338 32.465 1.00 27.33 ATOM 1743 C HIS A 750 1.615 −15.69131.475 1.00 16.04 ATOM 1744 O HIS A 750 2.521 −15.069 30.925 1.00 16.50ATOM 1745 N GLU A 751 0.680 −16.346 30.794 1.00 14.76 ATOM 1746 CA GLU A751 0.689 −16.359 29.333 1.00 14.97 ATOM 1747 CB GLU A 751 −0.269−17.427 28.798 1.00 11.89 ATOM 1748 CG GLU A 751 0.173 −18.848 29.1231.00 16.94 ATOM 1749 CD GLU A 751 −0.601 −19.892 28.354 1.00 17.06 ATOM1750 OE1 GLU A 751 −0.804 −19.697 27.140 1.00 17.15 ATOM 1751 OE2 GLU A751 −0.993 −20.912 28.959 1.00 27.83 ATOM 1752 C GLU A 751 0.325 −14.98828.764 1.00 14.11 ATOM 1753 O GLU A 751 0.782 −14.616 27.685 1.00 14.18ATOM 1754 N LYS A 752 −0.501 −14.248 29.498 1.00 13.06 ATOM 1755 CA LYSA 752 −0.900 −12.910 29.092 1.00 11.63 ATOM 1756 CB LYS A 752 −1.984−12.370 30.041 1.00 11.74 ATOM 1757 CG LYS A 752 −2.200 −10.865 29.9811.00 11.33 ATOM 1758 CD LYS A 752 −2.667 −10.402 28.608 1.00 18.51 ATOM1759 CE LYS A 752 −3.921 −11.138 28.184 1.00 31.49 ATOM 1760 NZ LYS A752 −4.536 −10.523 26.978 1.00 47.29 ATOM 1761 C LYS A 752 0.362 −12.04729.176 1.00 14.58 ATOM 1762 O LYS A 752 0.665 −11.293 28.249 1.00 11.11ATOM 1763 N GLU A 753 1.093 −12.196 30.270 1.00 12.46 ATOM 1764 CA GLU A753 2.315 −11.409 30.445 1.00 13.89 ATOM 1765 CB GLU A 753 2.939 −11.74531.801 1.00 15.41 ATOM 1766 CG GLU A 753 4.187 −10.950 32.098 1.00 17.51ATOM 1767 CD GLU A 753 4.946 −11.478 33.300 1.00 36.21 ATOM 1768 OE1 GLUA 753 4.335 −11.579 34.384 1.00 28.23 ATOM 1769 OE2 GLU A 753 6.150−11.782 33.162 1.00 36.81 ATOM 1770 C GLU A 753 3.267 −11.729 29.3131.00 14.45 ATOM 1771 O GLU A 753 3.852 −10.839 28.671 1.00 11.34 ATOM1772 N LEU A 754 3.441 −13.018 29.035 1.00 12.90 ATOM 1773 CA LEU A 7544.329 −13.471 27.974 1.00 13.51 ATOM 1774 CB LEU A 754 4.377 −15.01127.908 1.00 13.76 ATOM 1775 CG LEU A 754 5.196 −15.682 26.793 1.00 15.32ATOM 1776 CD1 LEU A 754 6.663 −15.286 26.877 1.00 15.56 ATOM 1777 CD2LEU A 754 5.044 −17.193 26.930 1.00 14.90 ATOM 1778 C LEU A 754 3.915−12.900 26.616 1.00 12.21 ATOM 1779 O LEU A 754 4.765 −12.478 25.8211.00 11.37 ATOM 1780 N PHE A 755 2.613 −12.867 26.351 1.00 11.00 ATOM1781 CA PHE A 755 2.119 −12.336 25.088 1.00 9.92 ATOM 1782 CB PHE A 7550.609 −12.551 24.966 1.00 12.44 ATOM 1783 CG PHE A 755 0.002 −11.86723.780 1.00 11.67 ATOM 1784 CD1 PHE A 755 0.338 −12.259 22.492 1.0013.36 ATOM 1785 CD2 PHE A 755 −0.858 −10.792 23.948 1.00 9.93 ATOM 1786CE1 PHE A 755 −0.170 −11.590 21.393 1.00 14.56 ATOM 1787 CE2 PHE A 755−1.369 −10.118 22.854 1.00 13.93 ATOM 1788 CZ PHE A 755 −1.021 −10.51721.574 1.00 18.65 ATOM 1789 C PHE A 755 2.431 −10.840 24.972 1.00 9.95ATOM 1790 O PHE A 755 2.856 −10.367 23.916 1.00 10.28 ATOM 1791 N LEU A756 2.225 −10.099 26.057 1.00 9.98 ATOM 1792 CA LEU A 756 2.489 −8.66426.034 1.00 9.03 ATOM 1793 CB LEU A 756 2.102 −8.017 27.370 1.00 9.14ATOM 1794 CG LEU A 756 0.610 −8.119 27.706 1.00 13.27 ATOM 1795 CD1 LEUA 756 0.331 −7.487 29.065 1.00 21.21 ATOM 1796 CD2 LEU A 756 −0.198−7.432 26.613 1.00 18.57 ATOM 1797 C LEU A 756 3.959 −8.410 25.721 1.009.36 ATOM 1798 O LEU A 756 4.291 −7.437 25.045 1.00 8.42 ATOM 1799 N ALAA 757 4.844 −9.285 26.197 1.00 7.41 ATOM 1800 CA ALA A 757 6.267 −9.11825.915 1.00 10.17 ATOM 1801 CB ALA A 757 7.096 −10.112 26.720 1.00 10.57ATOM 1802 C ALA A 757 6.514 −9.315 24.421 1.00 9.99 ATOM 1803 O ALA A757 7.254 −8.548 23.798 1.00 10.22 ATOM 1804 N MET A 758 5.890 −10.34123.845 1.00 8.41 ATOM 1805 CA MET A 758 6.046 −10.627 22.422 1.00 8.55ATOM 1806 CB MET A 758 5.348 −11.946 22.061 1.00 8.57 ATOM 1807 CG MET A758 5.898 −13.175 22.783 1.00 9.97 ATOM 1808 SD MET A 758 7.613 −13.59722.367 1.00 15.99 ATOM 1809 CE MET A 758 7.436 −14.226 20.702 1.00 36.66ATOM 1810 C MET A 758 5.469 −9.499 21.572 1.00 9.31 ATOM 1811 O MET A758 6.035 −9.134 20.534 1.00 8.67 ATOM 1812 N LEU A 759 4.334 −8.96222.008 1.00 10.68 ATOM 1813 CA LEU A 759 3.682 −7.877 21.290 1.00 7.26ATOM 1814 CB LEU A 759 2.348 −7.536 21.954 1.00 6.70 ATOM 1815 CG LEU A759 1.521 −6.419 21.316 1.00 9.88 ATOM 1816 CD1 LEU A 759 1.217 −6.75119.858 1.00 13.46 ATOM 1817 CD2 LEU A 759 0.232 −6.241 22.103 1.00 8.91ATOM 1818 C LEU A 759 4.589 −6.650 21.269 1.00 10.65 ATOM 1819 O LEU A759 4.677 −5.945 20.259 1.00 8.66 ATOM 1820 N MET A 760 5.258 −6.38822.387 1.00 8.87 ATOM 1821 CA MET A 760 6.168 −5.251 22.454 1.00 9.10ATOM 1822 CB MET A 760 6.760 −5.114 23.859 1.00 9.37 ATOM 1823 CG MET A760 5.831 −4.491 24.889 1.00 7.94 ATOM 1824 SD MET A 760 5.392 −2.76224.513 1.00 11.15 ATOM 1825 CE MET A 760 6.981 −1.951 24.748 1.00 10.58ATOM 1826 C MET A 760 7.292 −5.445 21.444 1.00 9.36 ATOM 1827 O MET A760 7.693 −4.501 20.757 1.00 8.44 ATOM 1828 N THR A 761 7.812 −6.66721.359 1.00 8.62 ATOM 1829 CA THR A 761 8.890 −6.948 20.416 1.00 9.46ATOM 1830 CB THR A 761 9.442 −8.379 20.597 1.00 12.42 ATOM 1831 OG1 THRA 761 9.916 −8.540 21.940 1.00 11.86 ATOM 1832 CG2 THR A 761 10.598−8.636 19.620 1.00 9.90 ATOM 1833 C THR A 761 8.389 −6.785 18.984 1.0010.31 ATOM 1834 O THR A 761 9.088 −6.238 18.128 1.00 10.55 ATOM 1835 NALA A 762 7.172 −7.254 18.722 1.00 10.42 ATOM 1836 CA ALA A 762 6.598−7.148 17.389 1.00 7.73 ATOM 1837 CB ALA A 762 5.202 −7.777 17.362 1.0010.79 ATOM 1838 C ALA A 762 6.524 −5.689 16.948 1.00 9.57 ATOM 1839 OALA A 762 6.794 −5.370 15.787 1.00 9.59 ATOM 1840 N CYS A 763 6.161−4.801 17.872 1.00 7.53 ATOM 1841 CA CYS A 763 6.063 −3.378 17.551 1.007.89 ATOM 1842 CB CYS A 763 5.237 −2.641 18.611 1.00 11.70 ATOM 1843 SGCYS A 763 3.503 −3.143 18.670 1.00 11.19 ATOM 1844 C CYS A 763 7.441−2.744 17.443 1.00 9.03 ATOM 1845 O CYS A 763 7.689 −1.911 16.574 1.0010.26 ATOM 1846 N ASP A 764 8.340 −3.157 18.329 1.00 8.73 ATOM 1847 CAASP A 764 9.703 −2.641 18.352 1.00 10.03 ATOM 1848 CB ASP A 764 10.448−3.269 19.541 1.00 11.85 ATOM 1849 CG ASP A 764 11.766 −2.585 19.8401.00 12.03 ATOM 1850 OD1 ASP A 764 11.963 −1.451 19.361 1.00 11.46 ATOM1851 OD2 ASP A 764 12.592 −3.176 20.571 1.00 15.03 ATOM 1852 C ASP A 76410.447 −2.924 17.036 1.00 10.20 ATOM 1853 O ASP A 764 11.225 −2.09716.562 1.00 11.71 ATOM 1854 N LEU A 765 10.194 −4.086 16.442 1.00 11.54ATOM 1855 CA LEU A 765 10.867 −4.474 15.202 1.00 11.71 ATOM 1856 CB LEUA 765 11.208 −5.965 15.252 1.00 13.42 ATOM 1857 CG LEU A 765 12.017−6.454 16.453 1.00 15.02 ATOM 1858 CD1 LEU A 765 12.233 −7.957 16.3481.00 13.91 ATOM 1859 CD2 LEU A 765 13.345 −5.721 16.499 1.00 16.31 ATOM1860 C LEU A 765 10.049 −4.221 13.941 1.00 12.10 ATOM 1861 O LEU A 76510.490 −4.560 12.837 1.00 11.30 ATOM 1862 N SER A 766 8.881 −3.60614.101 1.00 12.76 ATOM 1863 CA SER A 766 7.965 −3.383 12.983 1.00 10.86ATOM 1864 CB SER A 766 6.672 −2.733 13.488 1.00 8.49 ATOM 1865 OG SER A766 6.902 −1.438 13.991 1.00 14.83 ATOM 1866 C SER A 766 8.446 −2.65711.729 1.00 7.60 ATOM 1867 O SER A 766 7.782 −2.735 10.700 1.00 9.56ATOM 1868 N ALA A 767 9.575 −1.956 11.787 1.00 8.02 ATOM 1869 CA ALA A767 10.073 −1.296 10.581 1.00 9.45 ATOM 1870 CB ALA A 767 11.364 −0.52210.881 1.00 11.41 ATOM 1871 C ALA A 767 10.340 −2.377 9.521 1.00 10.04ATOM 1872 O ALA A 767 10.253 −2.124 8.319 1.00 10.04 ATOM 1873 N ILE A768 10.655 −3.586 9.976 1.00 9.49 ATOM 1874 CA ILE A 768 10.942 −4.6949.066 1.00 12.99 ATOM 1875 CB ILE A 768 11.555 −5.894 9.840 1.00 9.64ATOM 1876 CG2 ILE A 768 10.473 −6.631 10.612 1.00 7.91 ATOM 1877 CG1 ILEA 768 12.270 −6.836 8.868 1.00 12.83 ATOM 1878 CD1 ILE A 768 13.471−6.199 8.190 1.00 15.69 ATOM 1879 C ILE A 768 9.704 −5.173 8.296 1.0011.57 ATOM 1880 O ILE A 768 9.812 −5.986 7.376 1.00 12.45 ATOM 1881 NTHR A 769 8.530 −4.665 8.662 1.00 12.70 ATOM 1882 CA THR A 769 7.286−5.062 7.999 1.00 10.88 ATOM 1883 CB THR A 769 6.167 −5.326 9.025 1.0013.25 ATOM 1884 OG1 THR A 769 5.760 −4.083 9.617 1.00 12.15 ATOM 1885CG2 THR A 769 6.654 −6.271 10.124 1.00 16.86 ATOM 1886 C THR A 769 6.762−3.991 7.036 1.00 12.18 ATOM 1887 O THR A 769 5.795 −4.223 6.308 1.0013.18 ATOM 1888 N LYS A 770 7.402 −2.824 7.043 1.00 12.64 ATOM 1889 CALYS A 770 6.986 −1.686 6.216 1.00 10.43 ATOM 1890 CB LYS A 770 7.684−0.413 6.714 1.00 12.22 ATOM 1891 CG LYS A 770 7.375 −0.029 8.165 1.007.87 ATOM 1892 CD LYS A 770 5.948 0.457 8.330 1.00 13.33 ATOM 1893 CELYS A 770 5.644 0.766 9.794 1.00 14.40 ATOM 1894 NZ LYS A 770 4.2631.293 9.973 1.00 14.45 ATOM 1895 C LYS A 770 7.247 −1.829 4.716 1.0011.91 ATOM 1896 O LYS A 770 8.069 −2.638 4.290 1.00 13.63 ATOM 1897 NPRO A 771 6.529 −1.041 3.892 1.00 11.52 ATOM 1898 CD PRO A 771 5.408−0.150 4.240 1.00 14.60 ATOM 1899 CA PRO A 771 6.718 −1.096 2.441 1.0012.80 ATOM 1900 CB PRO A 771 5.914 0.099 1.950 1.00 15.88 ATOM 1901 CGPRO A 771 4.751 0.098 2.886 1.00 11.15 ATOM 1902 C PRO A 771 8.206−0.933 2.183 1.00 14.66 ATOM 1903 O PRO A 771 8.880 −0.201 2.908 1.0015.01 ATOM 1904 N TRP A 772 8.711 −1.604 1.156 1.00 14.26 ATOM 1905 CATRP A 772 10.133 −1.555 0.827 1.00 15.34 ATOM 1906 CB TRP A 772 10.367−2.121 −0.578 1.00 14.10 ATOM 1907 CG TRP A 772 11.809 −2.101 −1.0091.00 17.47 ATOM 1908 CD2 TRP A 772 12.931 −2.659 −0.307 1.00 17.61 ATOM1909 CE2 TRP A 772 14.079 −2.404 −1.086 1.00 19.63 ATOM 1910 CE3 TRP A772 13.076 −3.348 0.901 1.00 16.69 ATOM 1911 CD1 TRP A 772 12.313 −1.547−2.152 1.00 16.69 ATOM 1912 NE1 TRP A 772 13.675 −1.725 −2.204 1.0024.41 ATOM 1913 CZ2 TRP A 772 15.354 −2.816 −0.694 1.00 24.29 ATOM 1914CZ3 TRP A 772 14.344 −3.755 1.289 1.00 17.48 ATOM 1915 CH2 TRP A 77215.466 −3.488 0.493 1.00 21.25 ATOM 1916 C TRP A 772 10.820 −0.190 0.9521.00 17.78 ATOM 1917 O TRP A 772 11.834 −0.070 1.639 1.00 15.81 ATOM1918 N PRO A 773 10.286 0.853 0.291 1.00 19.35 ATOM 1919 CD PRO A 7739.132 0.877 −0.624 1.00 18.85 ATOM 1920 CA PRO A 773 10.909 2.180 0.3771.00 18.24 ATOM 1921 CB PRO A 773 9.926 3.068 −0.382 1.00 21.17 ATOM1922 CG PRO A 773 9.386 2.138 −1.422 1.00 23.60 ATOM 1923 C PRO A 77311.129 2.654 1.814 1.00 16.33 ATOM 1924 O PRO A 773 12.167 3.235 2.1401.00 16.01 ATOM 1925 N ILE A 774 10.143 2.406 2.668 1.00 16.23 ATOM 1926CA ILE A 774 10.228 2.805 4.066 1.00 15.30 ATOM 1927 CB ILE A 774 8.8512.670 4.751 1.00 15.99 ATOM 1928 CG2 ILE A 774 8.977 2.922 6.250 1.0013.24 ATOM 1929 CG1 ILE A 774 7.867 3.658 4.110 1.00 20.68 ATOM 1930 CD1ILE A 774 6.441 3.501 4.588 1.00 21.74 ATOM 1931 C ILE A 774 11.2641.958 4.804 1.00 16.31 ATOM 1932 O ILE A 774 12.133 2.491 5.497 1.0015.63 ATOM 1933 N GLN A 775 11.173 0.640 4.650 1.00 13.80 ATOM 1934 CAGLN A 775 12.120 −0.274 5.279 1.00 12.85 ATOM 1935 CB GLN A 775 11.786−1.727 4.901 1.00 13.34 ATOM 1936 CG GLN A 775 12.987 −2.688 4.921 1.0014.20 ATOM 1937 CD GLN A 775 13.582 −2.897 6.305 1.00 21.70 ATOM 1938OE1 GLN A 775 14.663 −3.472 6.441 1.00 13.81 ATOM 1939 NE2 GLN A 77512.880 −2.440 7.336 1.00 14.50 ATOM 1940 C GLN A 775 13.549 0.057 4.8771.00 13.13 ATOM 1941 O GLN A 775 14.458 0.060 5.694 1.00 12.67 ATOM 1942N GLN A 776 13.749 0.352 3.590 1.00 10.04 ATOM 1943 CA GLN A 776 15.0680.674 3.090 1.00 12.84 ATOM 1944 CB GLN A 776 15.004 0.820 1.564 1.0019.00 ATOM 1945 CG GLN A 776 16.326 0.943 0.890 1.00 25.33 ATOM 1946 CDGLN A 776 16.172 0.760 −0.595 1.00 36.37 ATOM 1947 OE1 GLN A 776 15.2581.315 −1.209 1.00 39.80 ATOM 1948 NE2 GLN A 776 17.058 −0.023 −1.1861.00 41.16 ATOM 1949 C GLN A 776 15.627 1.934 3.738 1.00 10.61 ATOM 1950O GLN A 776 16.796 1.988 4.109 1.00 13.39 ATOM 1951 N ARG A 777 14.7762.946 3.922 1.00 10.52 ATOM 1952 CA ARG A 777 15.199 4.197 4.534 1.0011.43 ATOM 1953 CB ARG A 777 14.090 5.253 4.419 1.00 15.26 ATOM 1954 CGARG A 777 14.487 6.607 4.948 1.00 20.06 ATOM 1955 CD ARG A 777 13.3437.586 4.765 1.00 25.19 ATOM 1956 NE ARG A 777 12.206 7.273 5.627 1.0034.37 ATOM 1957 CZ ARG A 777 12.232 7.359 6.954 1.00 35.62 ATOM 1958 NH1ARG A 777 13.340 7.747 7.575 1.00 37.87 ATOM 1959 NH2 ARG A 777 11.1497.068 7.661 1.00 29.66 ATOM 1960 C ARG A 777 15.560 3.979 5.997 1.0010.83 ATOM 1961 O ARG A 777 16.601 4.447 6.472 1.00 13.15 ATOM 1962 NILE A 778 14.715 3.238 6.705 1.00 12.38 ATOM 1963 CA ILE A 778 14.9532.944 8.112 1.00 13.18 ATOM 1964 CB ILE A 778 13.753 2.209 8.744 1.0015.50 ATOM 1965 CG2 ILE A 778 14.091 1.788 10.170 1.00 13.56 ATOM 1966CG1 ILE A 778 12.516 3.108 8.721 1.00 22.29 ATOM 1967 CD1 ILE A 77812.685 4.399 9.478 1.00 26.81 ATOM 1968 C ILE A 778 16.198 2.086 8.3051.00 12.49 ATOM 1969 O ILE A 778 16.963 2.298 9.245 1.00 12.70 ATOM 1970N ALA A 779 16.399 1.117 7.417 1.00 12.47 ATOM 1971 CA ALA A 779 17.5630.242 7.510 1.00 13.19 ATOM 1972 CB ALA A 779 17.538 −0.789 6.391 1.0014.05 ATOM 1973 C ALA A 779 18.856 1.051 7.452 1.00 13.71 ATOM 1974 OALA A 779 19.839 0.700 8.106 1.00 11.99 ATOM 1975 N GLU A 780 18.8582.131 6.672 1.00 14.86 ATOM 1976 CA GLU A 780 20.048 2.976 6.560 1.0013.62 ATOM 1977 CB GLU A 780 19.860 4.053 5.487 1.00 17.29 ATOM 1978 CGGLU A 780 19.742 3.519 4.075 1.00 30.45 ATOM 1979 CD GLU A 780 19.7444.628 3.038 1.00 42.90 ATOM 1980 OE1 GLU A 780 20.761 5.347 2.939 1.0042.08 ATOM 1981 OE2 GLU A 780 18.728 4.783 2.326 1.00 56.88 ATOM 1982 CGLU A 780 20.350 3.649 7.897 1.00 13.45 ATOM 1983 O GLU A 780 21.5063.791 8.277 1.00 14.75 ATOM 1984 N LEU A 781 19.303 4.074 8.597 1.0012.82 ATOM 1985 CA LEU A 781 19.464 4.716 9.898 1.00 10.66 ATOM 1986 CBLEU A 781 18.113 5.215 10.410 1.00 12.60 ATOM 1987 CG LEU A 781 17.4286.296 9.574 1.00 15.49 ATOM 1988 CD1 LEU A 781 16.101 6.670 10.215 1.0014.52 ATOM 1989 CD2 LEU A 781 18.339 7.513 9.475 1.00 17.00 ATOM 1990 CLEU A 781 20.032 3.704 10.887 1.00 12.39 ATOM 1991 O LEU A 781 20.9354.014 11.673 1.00 11.98 ATOM 1992 N VAL A 782 19.490 2.490 10.839 1.009.90 ATOM 1993 CA VAL A 782 19.933 1.418 11.719 1.00 9.65 ATOM 1994 CBVAL A 782 19.116 0.126 11.463 1.00 10.42 ATOM 1995 CG1 VAL A 782 19.714−1.029 12.240 1.00 13.17 ATOM 1996 CG2 VAL A 782 17.657 0.339 11.8681.00 16.63 ATOM 1997 C VAL A 782 21.418 1.154 11.477 1.00 10.70 ATOM1998 O VAL A 782 22.210 1.068 12.418 1.00 13.37 ATOM 1999 N ALA A 78321.793 1.053 10.206 1.00 11.25 ATOM 2000 CA ALA A 783 23.185 0.810 9.8391.00 11.83 ATOM 2001 CB ALA A 783 23.299 0.632 8.337 1.00 15.10 ATOM2002 C ALA A 783 24.074 1.961 10.298 1.00 12.03 ATOM 2003 O ALA A 78325.170 1.746 10.820 1.00 12.81 ATOM 2004 N THR A 784 23.599 3.187 10.0991.00 11.94 ATOM 2005 CA THR A 784 24.358 4.359 10.504 1.00 10.90 ATOM2006 CB THR A 784 23.572 5.659 10.211 1.00 12.78 ATOM 2007 OG1 THR A 78423.359 5.778 8.797 1.00 15.62 ATOM 2008 CG2 THR A 784 24.341 6.88310.706 1.00 13.70 ATOM 2009 C THR A 784 24.676 4.282 11.995 1.00 11.74ATOM 2010 O THR A 784 25.819 4.490 12.408 1.00 10.51 ATOM 2011 N GLU A785 23.670 3.969 12.805 1.00 10.01 ATOM 2012 CA GLU A 785 23.881 3.88014.243 1.00 10.75 ATOM 2013 CB GLU A 785 22.549 3.669 14.968 1.00 7.51ATOM 2014 CG GLU A 785 22.675 3.740 16.483 1.00 9.65 ATOM 2015 CD GLU A785 21.335 3.755 17.178 1.00 7.52 ATOM 2016 OE1 GLU A 785 20.415 4.43616.674 1.00 10.93 ATOM 2017 OE2 GLU A 785 21.208 3.099 18.236 1.00 12.56ATOM 2018 C GLU A 785 24.847 2.760 14.612 1.00 11.99 ATOM 2019 O GLU A785 25.737 2.948 15.440 1.00 11.68 ATOM 2020 N PHE A 786 24.671 1.59413.997 1.00 9.83 ATOM 2021 CA PHE A 786 25.541 0.464 14.285 1.00 10.39ATOM 2022 CB PHE A 786 25.069 −0.794 13.550 1.00 11.58 ATOM 2023 CG PHEA 786 23.876 −1.455 14.176 1.00 16.59 ATOM 2024 CD1 PHE A 786 23.632−1.327 15.533 1.00 18.18 ATOM 2025 CD2 PHE A 786 23.034 −2.254 13.4191.00 19.90 ATOM 2026 CE1 PHE A 786 22.570 −1.986 16.125 1.00 25.35 ATOM2027 CE2 PHE A 786 21.972 −2.916 14.004 1.00 17.12 ATOM 2028 CZ PHE A786 21.740 −2.781 15.360 1.00 16.84 ATOM 2029 C PHE A 786 26.985 0.76013.898 1.00 9.62 ATOM 2030 O PHE A 786 27.907 0.444 14.652 1.00 10.46ATOM 2031 N PHE A 787 27.183 1.348 12.720 1.00 8.90 ATOM 2032 CA PHE A787 28.531 1.680 12.273 1.00 9.83 ATOM 2033 CB PHE A 787 28.515 2.14110.809 1.00 10.96 ATOM 2034 CG PHE A 787 28.116 1.056 9.849 1.00 8.28ATOM 2035 CD1 PHE A 787 28.335 −0.276 10.172 1.00 10.72 ATOM 2036 CD2PHE A 787 27.546 1.357 8.626 1.00 11.47 ATOM 2037 CE1 PHE A 787 27.993−1.287 9.296 1.00 12.45 ATOM 2038 CE2 PHE A 787 27.201 0.344 7.739 1.0012.21 ATOM 2039 CZ PHE A 787 27.424 −0.977 8.075 1.00 8.97 ATOM 2040 CPHE A 787 29.165 2.747 13.149 1.00 12.00 ATOM 2041 O PHE A 787 30.3872.787 13.311 1.00 11.70 ATOM 2042 N ASP A 788 28.340 3.620 13.713 1.0010.51 ATOM 2043 CA ASP A 788 28.867 4.655 14.583 1.00 13.07 ATOM 2044 CBASP A 788 27.770 5.654 14.953 1.00 9.28 ATOM 2045 CG ASP A 788 28.2756.751 15.869 1.00 17.65 ATOM 2046 OD1 ASP A 788 27.862 6.784 17.046 1.0022.26 ATOM 2047 OD2 ASP A 788 29.097 7.575 15.414 1.00 23.70 ATOM 2048 CASP A 788 29.427 3.975 15.832 1.00 11.61 ATOM 2049 O ASP A 788 30.4914.349 16.324 1.00 11.23 ATOM 2050 N GLN A 789 28.719 2.965 16.338 1.0010.39 ATOM 2051 CA GLN A 789 29.201 2.243 17.515 1.00 10.66 ATOM 2052 CBGLN A 789 28.185 1.199 17.979 1.00 14.04 ATOM 2053 CG GLN A 789 28.6670.416 19.191 1.00 13.95 ATOM 2054 CD GLN A 789 27.696 −0.652 19.641 1.0013.88 ATOM 2055 OE1 GLN A 789 26.488 −0.445 19.641 1.00 10.68 ATOM 2056NE2 GLN A 789 28.226 −1.799 20.051 1.00 10.88 ATOM 2057 C GLN A 78930.509 1.541 17.155 1.00 12.25 ATOM 2058 O GLN A 789 31.452 1.504 17.9521.00 12.92 ATOM 2059 N GLY A 790 30.552 0.979 15.950 1.00 12.27 ATOM2060 CA GLY A 790 31.746 0.292 15.493 1.00 13.69 ATOM 2061 C GLY A 79032.948 1.218 15.519 1.00 12.41 ATOM 2062 O GLY A 790 34.050 0.805 15.8851.00 14.19 ATOM 2063 N ASP A 791 32.743 2.476 15.135 1.00 13.24 ATOM2064 CA ASP A 791 33.837 3.448 15.135 1.00 15.89 ATOM 2065 CB ASP A 79133.383 4.802 14.582 1.00 11.78 ATOM 2066 CG ASP A 791 33.022 4.74813.108 1.00 11.72 ATOM 2067 OD1 ASP A 791 33.525 3.853 12.401 1.00 16.07ATOM 2068 OD2 ASP A 791 32.249 5.619 12.657 1.00 16.56 ATOM 2069 C ASP A791 34.350 3.653 16.554 1.00 15.06 ATOM 2070 O ASP A 791 35.555 3.75116.794 1.00 15.97 ATOM 2071 N ARG A 792 33.423 3.723 17.496 1.00 16.00ATOM 2072 CA ARG A 792 33.783 3.925 18.885 1.00 13.38 ATOM 2073 CB ARG A792 32.544 4.308 19.680 1.00 15.67 ATOM 2074 CG ARG A 792 32.056 5.68919.304 1.00 20.98 ATOM 2075 CD ARG A 792 30.791 6.043 20.014 1.00 22.55ATOM 2076 NE ARG A 792 30.929 6.004 21.465 1.00 21.96 ATOM 2077 CZ ARG A792 29.945 6.332 22.290 1.00 19.00 ATOM 2078 NH1 ARG A 792 28.782 6.72621.791 1.00 18.95 ATOM 2079 NH2 ARG A 792 30.105 6.236 23.601 1.00 23.88ATOM 2080 C ARG A 792 34.466 2.716 19.501 1.00 13.13 ATOM 2081 O ARG A792 35.296 2.865 20.390 1.00 14.33 ATOM 2082 N GLU A 793 34.112 1.52219.036 1.00 14.11 ATOM 2083 CA GLU A 793 34.730 0.305 19.545 1.00 12.55ATOM 2084 CB GLU A 793 33.969 −0.932 19.051 1.00 12.93 ATOM 2085 CG GLUA 793 32.531 −0.986 19.543 1.00 15.09 ATOM 2086 CD GLU A 793 31.816−2.269 19.165 1.00 17.10 ATOM 2087 OE1 GLU A 793 32.105 −2.807 18.0781.00 14.75 ATOM 2088 OE2 GLU A 793 30.951 −2.728 19.949 1.00 13.37 ATOM2089 C GLU A 793 36.184 0.251 19.080 1.00 13.70 ATOM 2090 O GLU A 79337.073 −0.143 19.837 1.00 14.48 ATOM 2091 N ARG A 794 36.429 0.65517.838 1.00 12.88 ATOM 2092 CA ARG A 794 37.792 0.647 17.318 1.00 16.50ATOM 2093 CB ARG A 794 37.828 1.083 15.847 1.00 16.91 ATOM 2094 CG ARG A794 37.330 0.047 14.838 1.00 16.40 ATOM 2095 CD ARG A 794 37.399 0.60913.422 1.00 20.95 ATOM 2096 NE ARG A 794 36.790 −0.268 12.422 1.00 21.25ATOM 2097 CZ ARG A 794 37.323 −1.407 11.996 1.00 16.41 ATOM 2098 NH1 ARGA 794 38.486 −1.822 12.480 1.00 26.91 ATOM 2099 NH2 ARG A 794 36.691−2.134 11.082 1.00 18.30 ATOM 2100 C ARG A 794 38.648 1.603 18.141 1.0017.48 ATOM 2101 O ARG A 794 39.781 1.287 18.503 1.00 18.61 ATOM 2102 NLYS A 795 38.087 2.769 18.443 1.00 19.00 ATOM 2103 CA LYS A 795 38.7933.795 19.199 1.00 19.03 ATOM 2104 CB LYS A 795 38.146 5.161 18.947 1.0022.77 ATOM 2105 CG LYS A 795 38.839 6.312 19.661 1.00 30.54 ATOM 2106 CDLYS A 795 38.128 7.633 19.410 1.00 38.45 ATOM 2107 CE LYS A 795 38.9028.796 20.009 1.00 34.57 ATOM 2108 NZ LYS A 795 40.267 8.886 19.424 1.0042.21 ATOM 2109 C LYS A 795 38.866 3.554 20.704 1.00 19.86 ATOM 2110 OLYS A 795 39.923 3.716 21.310 1.00 21.68 ATOM 2111 N GLU A 796 37.7473.166 21.304 1.00 17.50 ATOM 2112 CA GLU A 796 37.696 2.953 22.745 1.0018.20 ATOM 2113 CB GLU A 796 36.286 3.272 23.255 1.00 16.63 ATOM 2114 CGGLU A 796 35.872 4.722 23.048 1.00 19.55 ATOM 2115 CD GLU A 796 34.4254.982 23.414 1.00 17.22 ATOM 2116 OE1 GLU A 796 33.986 4.520 24.489 1.0017.11 ATOM 2117 OE2 GLU A 796 33.729 5.660 22.629 1.00 17.31 ATOM 2118 CGLU A 796 38.116 1.568 23.238 1.00 18.82 ATOM 2119 O GLU A 796 38.6041.432 24.359 1.00 19.88 ATOM 2120 N LEU A 797 37.936 0.544 22.408 1.0017.76 ATOM 2121 CA LEU A 797 38.279 −0.817 22.809 1.00 17.55 ATOM 2122CB LEU A 797 37.032 −1.708 22.732 1.00 14.21 ATOM 2123 CG LEU A 79735.816 −1.230 23.535 1.00 21.04 ATOM 2124 CD1 LEU A 797 34.655 −2.19423.333 1.00 19.81 ATOM 2125 CD2 LEU A 797 36.177 −1.134 25.008 1.0022.47 ATOM 2126 C LEU A 797 39.400 −1.441 21.980 1.00 18.06 ATOM 2127 OLEU A 797 39.899 −2.518 22.312 1.00 18.10 ATOM 2128 N ASN A 798 39.795−0.760 20.910 1.00 17.87 ATOM 2129 CA ASN A 798 40.846 −1.244 20.0161.00 17.14 ATOM 2130 CB ASN A 798 42.202 −1.278 20.732 1.00 18.53 ATOM2131 CG ASN A 798 43.357 −1.501 19.770 1.00 19.84 ATOM 2132 OD1 ASN A798 43.497 −0.774 18.788 1.00 22.65 ATOM 2133 ND2 ASN A 798 44.186−2.507 20.043 1.00 17.46 ATOM 2134 C ASN A 798 40.522 −2.632 19.472 1.0019.40 ATOM 2135 O ASN A 798 41.400 −3.485 19.352 1.00 18.37 ATOM 2136 NILE A 799 39.254 −2.852 19.141 1.00 18.23 ATOM 2137 CA ILE A 799 38.816−4.134 18.603 1.00 20.72 ATOM 2138 CB ILE A 799 37.779 −4.811 19.5291.00 23.69 ATOM 2139 CG2 ILE A 799 38.348 −4.970 20.930 1.00 25.12 ATOM2140 CG1 ILE A 799 36.500 −3.968 19.570 1.00 27.29 ATOM 2141 CD1 ILE A799 35.381 −4.581 20.373 1.00 23.09 ATOM 2142 C ILE A 799 38.158 −3.92617.243 1.00 20.66 ATOM 2143 O ILE A 799 37.636 −2.846 16.956 1.00 20.48ATOM 2144 N GLU A 800 38.199 −4.951 16.399 1.00 20.84 ATOM 2145 CA GLU A800 37.558 −4.855 15.096 1.00 19.43 ATOM 2146 CB GLU A 800 38.162 −5.85614.109 1.00 25.89 ATOM 2147 CG GLU A 800 37.507 −5.813 12.735 1.00 37.89ATOM 2148 CD GLU A 800 38.245 −6.637 11.699 1.00 48.08 ATOM 2149 OE1 GLUA 800 38.421 −7.856 11.915 1.00 47.23 ATOM 2150 OE2 GLU A 800 38.647−6.063 10.663 1.00 52.27 ATOM 2151 C GLU A 800 36.095 −5.188 15.345 1.0016.86 ATOM 2152 O GLU A 800 35.774 −6.249 15.879 1.00 20.00 ATOM 2153 NPRO A 801 35.186 −4.277 14.979 1.00 16.72 ATOM 2154 CD PRO A 801 35.413−2.971 14.340 1.00 13.94 ATOM 2155 CA PRO A 801 33.755 −4.518 15.1881.00 15.17 ATOM 2156 CB PRO A 801 33.101 −3.242 14.651 1.00 11.35 ATOM2157 CG PRO A 801 34.189 −2.204 14.760 1.00 18.39 ATOM 2158 C PRO A 80133.249 −5.750 14.446 1.00 14.88 ATOM 2159 O PRO A 801 33.836 −6.16813.437 1.00 14.57 ATOM 2160 N THR A 802 32.166 −6.333 14.952 1.00 13.89ATOM 2161 CA THR A 802 31.554 −7.473 14.282 1.00 13.70 ATOM 2162 CB THRA 802 30.367 −8.057 15.090 1.00 18.66 ATOM 2163 OG1 THR A 802 29.339−7.067 15.227 1.00 22.82 ATOM 2164 CG2 THR A 802 30.824 −8.491 16.4751.00 28.52 ATOM 2165 C THR A 802 31.028 −6.886 12.974 1.00 13.06 ATOM2166 O THR A 802 30.896 −5.666 12.853 1.00 13.12 ATOM 2167 N ASP A 80330.730 −7.737 11.997 1.00 13.68 ATOM 2168 CA ASP A 803 30.239 −7.26010.706 1.00 13.10 ATOM 2169 CB ASP A 803 29.784 −8.436 9.840 1.00 15.94ATOM 2170 CG ASP A 803 30.942 −9.281 9.340 1.00 19.70 ATOM 2171 OD1 ASPA 803 32.108 −8.965 9.661 1.00 16.86 ATOM 2172 OD2 ASP A 803 30.681−10.265 8.619 1.00 17.57 ATOM 2173 C ASP A 803 29.092 −6.262 10.829 1.0014.26 ATOM 2174 O ASP A 803 29.071 −5.239 10.141 1.00 15.59 ATOM 2175 NLEU A 804 28.142 −6.561 11.706 1.00 12.76 ATOM 2176 CA LEU A 804 26.982−5.700 11.907 1.00 13.21 ATOM 2177 CB LEU A 804 26.116 −6.251 13.0421.00 14.65 ATOM 2178 CG LEU A 804 24.861 −5.430 13.347 1.00 15.24 ATOM2179 CD1 LEU A 804 24.020 −5.317 12.092 1.00 16.29 ATOM 2180 CD2 LEU A804 24.068 −6.089 14.461 1.00 23.77 ATOM 2181 C LEU A 804 27.356 −4.25212.214 1.00 13.48 ATOM 2182 O LEU A 804 26.646 −3.317 11.825 1.00 13.22ATOM 2183 N MET A 805 28.476 −4.067 12.904 1.00 12.28 ATOM 2184 CA MET A805 28.909 −2.725 13.276 1.00 11.75 ATOM 2185 CB MET A 805 29.141 −2.67114.790 1.00 13.28 ATOM 2186 CG MET A 805 27.859 −2.865 15.589 1.00 33.42ATOM 2187 SD MET A 805 28.125 −3.166 17.338 1.00 47.91 ATOM 2188 CE META 805 26.447 −3.244 17.925 1.00 28.62 ATOM 2189 C MET A 805 30.160−2.268 12.542 1.00 11.31 ATOM 2190 O MET A 805 30.761 −1.259 12.908 1.0012.42 ATOM 2191 N ASN A 806 30.530 −2.992 11.490 1.00 11.94 ATOM 2192 CAASN A 806 31.726 −2.673 10.712 1.00 13.21 ATOM 2193 CB ASN A 806 32.537−3.954 10.471 1.00 13.42 ATOM 2194 CG ASN A 806 33.907 −3.676 9.876 1.0016.11 ATOM 2195 OD1 ASN A 806 34.209 −2.549 9.484 1.00 17.92 ATOM 2196ND2 ASN A 806 34.740 −4.706 9.802 1.00 15.54 ATOM 2197 C ASN A 80631.371 −2.023 9.374 1.00 14.20 ATOM 2198 O ASN A 806 30.988 −2.715 8.4301.00 14.08 ATOM 2199 N ARG A 807 31.508 −0.699 9.296 1.00 12.56 ATOM2200 CA ARG A 807 31.189 0.037 8.075 1.00 14.91 ATOM 2201 CB ARG A 80731.410 1.543 8.275 1.00 16.99 ATOM 2202 CG ARG A 807 30.891 2.385 7.1161.00 25.83 ATOM 2203 CD ARG A 807 31.162 3.881 7.280 1.00 30.30 ATOM2204 NE ARG A 807 30.520 4.470 8.457 1.00 20.02 ATOM 2205 CZ ARG A 80731.078 4.525 9.662 1.00 16.27 ATOM 2206 NH1 ARG A 807 32.290 4.025 9.8541.00 20.90 ATOM 2207 NH2 ARG A 807 30.431 5.095 10.670 1.00 15.75 ATOM2208 C ARG A 807 32.021 −0.442 6.889 1.00 13.89 ATOM 2209 O ARG A 80731.573 −0.392 5.736 1.00 13.84 ATOM 2210 N GLU A 808 33.228 −0.910 7.1771.00 11.68 ATOM 2211 CA GLU A 808 34.122 −1.397 6.137 1.00 17.06 ATOM2212 CB GLU A 808 35.502 −1.675 6.731 1.00 16.87 ATOM 2213 CG GLU A 80836.256 −0.394 7.085 1.00 22.64 ATOM 2214 CD GLU A 808 37.556 −0.6457.819 1.00 24.85 ATOM 2215 OE1 GLU A 808 38.293 −1.576 7.430 1.00 26.32ATOM 2216 OE2 GLU A 808 37.846 0.100 8.780 1.00 36.15 ATOM 2217 C GLU A808 33.565 −2.641 5.461 1.00 15.58 ATOM 2218 O GLU A 808 33.929 −2.9564.329 1.00 15.69 ATOM 2219 N LYS A 809 32.677 −3.343 6.156 1.00 14.84ATOM 2220 CA LYS A 809 32.062 −4.544 5.600 1.00 16.67 ATOM 2221 CB LYS A809 32.381 −5.765 6.478 1.00 12.30 ATOM 2222 CG LYS A 809 33.845 −6.1846.405 1.00 13.87 ATOM 2223 CD LYS A 809 34.151 −7.408 7.259 1.00 14.82ATOM 2224 CE LYS A 809 33.430 −8.641 6.745 1.00 25.64 ATOM 2225 NZ LYS A809 33.789 −9.854 7.534 1.00 21.95 ATOM 2226 C LYS A 809 30.555 −4.3635.445 1.00 15.95 ATOM 2227 O LYS A 809 29.770 −5.281 5.693 1.00 18.05ATOM 2228 N LYS A 810 30.156 −3.167 5.022 1.00 15.13 ATOM 2229 CA LYS A810 28.742 −2.867 4.828 1.00 16.24 ATOM 2230 CB LYS A 810 28.549 −1.3834.494 1.00 14.35 ATOM 2231 CG LYS A 810 29.347 −0.869 3.312 1.00 24.48ATOM 2232 CD LYS A 810 29.222 0.647 3.226 1.00 29.64 ATOM 2233 CE LYS A810 29.994 1.224 2.049 1.00 35.68 ATOM 2234 NZ LYS A 810 29.432 0.7860.746 1.00 42.39 ATOM 2235 C LYS A 810 28.139 −3.744 3.734 1.00 14.42ATOM 2236 O LYS A 810 26.921 −3.843 3.607 1.00 14.44 ATOM 2237 N ASN A811 28.995 −4.389 2.950 1.00 13.62 ATOM 2238 CA ASN A 811 28.511 −5.2701.893 1.00 13.60 ATOM 2239 CB ASN A 811 29.680 −5.746 1.016 1.00 18.14ATOM 2240 CG ASN A 811 30.815 −6.340 1.826 1.00 21.65 ATOM 2241 OD1 ASNA 811 30.936 −7.559 1.958 1.00 17.54 ATOM 2242 ND2 ASN A 811 31.651−5.472 2.388 1.00 13.93 ATOM 2243 C ASN A 811 27.777 −6.474 2.487 1.0014.60 ATOM 2244 O ASN A 811 27.084 −7.197 1.777 1.00 13.25 ATOM 2245 NLYS A 812 27.922 −6.677 3.796 1.00 14.05 ATOM 2246 CA LYS A 812 27.279−7.797 4.478 1.00 15.17 ATOM 2247 CB LYS A 812 28.057 −8.150 5.753 1.0015.23 ATOM 2248 CG LYS A 812 29.401 −8.803 5.500 1.00 20.27 ATOM 2249 CDLYS A 812 29.198 −10.137 4.817 1.00 28.44 ATOM 2250 CE LYS A 812 30.497−10.886 4.658 1.00 35.44 ATOM 2251 NZ LYS A 812 30.257 −12.223 4.0481.00 38.51 ATOM 2252 C LYS A 812 25.818 −7.542 4.859 1.00 15.78 ATOM2253 O LYS A 812 25.109 −8.475 5.258 1.00 13.98 ATOM 2254 N ILE A 81325.366 −6.297 4.724 1.00 14.64 ATOM 2255 CA ILE A 813 24.012 −5.9645.144 1.00 14.83 ATOM 2256 CB ILE A 813 23.770 −4.460 5.007 1.00 15.21ATOM 2257 CG2 ILE A 813 22.264 −4.158 5.091 1.00 15.81 ATOM 2258 CG1 ILEA 813 24.616 −3.740 6.073 1.00 13.99 ATOM 2259 CD1 ILE A 813 24.445−2.265 6.070 1.00 27.43 ATOM 2260 C ILE A 813 22.862 −6.792 4.546 1.0014.67 ATOM 2261 O ILE A 813 22.042 −7.309 5.270 1.00 13.44 ATOM 2262 NPRO A 814 22.807 −6.936 3.224 1.00 12.07 ATOM 2263 CD PRO A 814 23.603−6.274 2.191 1.00 14.86 ATOM 2264 CA PRO A 814 21.709 −7.724 2.623 1.0014.39 ATOM 2265 CB PRO A 814 22.060 −7.714 1.152 1.00 13.45 ATOM 2266 CGPRO A 814 22.693 −6.351 1.001 1.00 14.67 ATOM 2267 C PRO A 814 21.605−9.144 3.185 1.00 11.82 ATOM 2268 O PRO A 814 20.525 −9.603 3.570 1.0012.87 ATOM 2269 N SER A 815 22.730 −9.846 3.215 1.00 11.71 ATOM 2270 CASER A 815 22.730 −11.205 3.729 1.00 13.13 ATOM 2271 CB SER A 815 24.102−11.863 3.526 1.00 14.66 ATOM 2272 OG SER A 815 25.124 −11.185 4.2331.00 27.24 ATOM 2273 C SER A 815 22.366 −11.220 5.212 1.00 14.09 ATOM2274 O SER A 815 21.677 −12.120 5.682 1.00 14.61 ATOM 2275 N MET A 81622.809 −10.211 5.937 1.00 14.82 ATOM 2276 CA MET A 816 22.498 −10.1977.353 1.00 14.08 ATOM 2277 CB MET A 816 23.449 −9.254 8.079 1.00 16.95ATOM 2278 CG MET A 816 24.829 −9.872 8.232 1.00 19.08 ATOM 2279 SD MET A816 26.019 −8.905 9.168 1.00 23.16 ATOM 2280 CE MET A 816 25.502 −9.31010.812 1.00 29.41 ATOM 2281 C MET A 816 21.057 −9.838 7.628 1.00 12.78ATOM 2282 O MET A 816 20.477 −10.281 8.613 1.00 13.06 ATOM 2283 N GLN A817 20.464 −9.010 6.765 1.00 11.62 ATOM 2284 CA GLN A 817 19.061 −8.6376.915 1.00 11.33 ATOM 2285 CB GLN A 817 18.666 −7.547 5.899 1.00 12.94ATOM 2286 CG GLN A 817 19.186 −6.179 6.283 1.00 11.95 ATOM 2287 CD GLN A817 18.469 −5.624 7.500 1.00 17.94 ATOM 2288 OE1 GLN A 817 18.544 −6.1838.595 1.00 34.56 ATOM 2289 NE2 GLN A 817 17.759 −4.523 7.309 1.00 34.13ATOM 2290 C GLN A 817 18.202 −9.882 6.714 1.00 13.31 ATOM 2291 O GLN A817 17.254 −10.116 7.472 1.00 10.14 ATOM 2292 N VAL A 818 18.537 −10.6985.715 1.00 12.18 ATOM 2293 CA VAL A 818 17.774 −11.918 5.479 1.00 11.53ATOM 2294 CB VAL A 818 18.252 −12.659 4.210 1.00 13.56 ATOM 2295 CG1 VALA 818 17.500 −13.972 4.063 1.00 10.58 ATOM 2296 CG2 VAL A 818 18.032−11.781 2.982 1.00 17.92 ATOM 2297 C VAL A 818 17.903 −12.858 6.678 1.0011.51 ATOM 2298 O VAL A 818 16.930 −13.494 7.090 1.00 12.55 ATOM 2299 NGLY A 819 19.110 −12.934 7.231 1.00 11.44 ATOM 2300 CA GLY A 819 19.356−13.791 8.376 1.00 12.74 ATOM 2301 C GLY A 819 18.556 −13.335 9.579 1.0013.96 ATOM 2302 O GLY A 819 18.068 −14.149 10.360 1.00 13.49 ATOM 2303 NPHE A 820 18.430 −12.022 9.725 1.00 14.20 ATOM 2304 CA PHE A 820 17.682−11.426 10.825 1.00 11.70 ATOM 2305 CB PHE A 820 17.927 −9.913 10.8331.00 11.32 ATOM 2306 CG PHE A 820 17.122 −9.167 11.858 1.00 9.99 ATOM2307 CD1 PHE A 820 17.268 −9.436 13.209 1.00 23.52 ATOM 2308 CD2 PHE A820 16.225 −8.184 11.466 1.00 17.26 ATOM 2309 CE1 PHE A 820 16.529−8.740 14.151 1.00 19.87 ATOM 2310 CE2 PHE A 820 15.485 −7.488 12.4031.00 16.59 ATOM 2311 CZ PHE A 820 15.640 −7.767 13.746 1.00 17.66 ATOM2312 C PHE A 820 16.191 −11.731 10.651 1.00 12.70 ATOM 2313 O PHE A 82015.498 −12.103 11.604 1.00 10.72 ATOM 2314 N ILE A 821 15.697 −11.5719.429 1.00 10.04 ATOM 2315 CA ILE A 821 14.298 −11.850 9.150 1.00 9.29ATOM 2316 CB ILE A 821 13.957 −11.540 7.679 1.00 10.14 ATOM 2317 CG2 ILEA 821 12.617 −12.166 7.307 1.00 12.87 ATOM 2318 CG1 ILE A 821 13.931−10.022 7.479 1.00 12.03 ATOM 2319 CD1 ILE A 821 13.795 −9.580 6.0371.00 14.77 ATOM 2320 C ILE A 821 13.991 −13.311 9.462 1.00 11.67 ATOM2321 O ILE A 821 13.012 −13.617 10.140 1.00 11.27 ATOM 2322 N ASP A 82214.841 −14.215 8.985 1.00 11.97 ATOM 2323 CA ASP A 822 14.634 −15.6379.237 1.00 14.30 ATOM 2324 CB ASP A 822 15.630 −16.479 8.428 1.00 17.59ATOM 2325 CG ASP A 822 15.317 −16.499 6.942 1.00 17.92 ATOM 2326 OD1 ASPA 822 14.177 −16.153 6.564 1.00 15.98 ATOM 2327 OD2 ASP A 822 16.212−16.880 6.152 1.00 13.97 ATOM 2328 C ASP A 822 14.759 −16.021 10.7141.00 15.42 ATOM 2329 O ASP A 822 13.876 −16.671 11.275 1.00 16.53 ATOM2330 N ALA A 823 15.849 −15.608 11.345 1.00 13.55 ATOM 2331 CA ALA A 82316.101 −15.971 12.737 1.00 15.03 ATOM 2332 CB ALA A 823 17.580 −15.75613.058 1.00 13.84 ATOM 2333 C ALA A 823 15.254 −15.299 13.810 1.00 15.13ATOM 2334 O ALA A 823 14.907 −15.928 14.810 1.00 17.91 ATOM 2335 N ILE A824 14.914 −14.032 13.606 1.00 13.91 ATOM 2336 CA ILE A 824 14.169−13.281 14.611 1.00 14.87 ATOM 2337 CB ILE A 824 14.929 −11.971 14.9661.00 16.51 ATOM 2338 CG2 ILE A 824 14.085 −11.106 15.891 1.00 11.92 ATOM2339 CG1 ILE A 824 16.291 −12.293 15.589 1.00 19.03 ATOM 2340 CD1 ILE A824 16.211 −12.966 16.938 1.00 17.79 ATOM 2341 C ILE A 824 12.736−12.872 14.271 1.00 15.38 ATOM 2342 O ILE A 824 11.817 −13.051 15.0771.00 15.58 ATOM 2343 N CYS A 825 12.548 −12.332 13.074 1.00 11.66 ATOM2344 CA CYS A 825 11.248 −11.798 12.682 1.00 10.83 ATOM 2345 CB CYS A825 11.470 −10.717 11.629 1.00 14.06 ATOM 2346 SG CYS A 825 12.684−9.498 12.156 1.00 12.72 ATOM 2347 C CYS A 825 10.094 −12.685 12.2311.00 12.83 ATOM 2348 O CYS A 825 9.003 −12.606 12.792 1.00 11.78 ATOM2349 N LEU A 826 10.312 −13.508 11.213 1.00 10.64 ATOM 2350 CA LEU A 8269.230 −14.343 10.699 1.00 12.29 ATOM 2351 CB LEU A 826 9.759 −15.2919.621 1.00 17.45 ATOM 2352 CG LEU A 826 10.132 −14.585 8.314 1.00 14.44ATOM 2353 CD1 LEU A 826 10.756 −15.585 7.355 1.00 19.69 ATOM 2354 CD2LEU A 826 8.884 −13.965 7.693 1.00 17.13 ATOM 2355 C LEU A 826 8.428−15.131 11.735 1.00 11.75 ATOM 2356 O LEU A 826 7.194 −15.094 11.7281.00 12.87 ATOM 2357 N GLN A 827 9.115 −15.842 12.620 1.00 9.56 ATOM2358 CA GLN A 827 8.426 −16.637 13.632 1.00 10.96 ATOM 2359 CB GLN A 8279.438 −17.368 14.507 1.00 9.95 ATOM 2360 CG GLN A 827 10.207 −18.46513.805 1.00 14.60 ATOM 2361 CD GLN A 827 11.365 −18.949 14.646 1.0027.21 ATOM 2362 OE1 GLN A 827 12.420 −18.312 14.695 1.00 20.68 ATOM 2363NE2 GLN A 827 11.169 −20.068 15.335 1.00 24.19 ATOM 2364 C GLN A 8277.516 −15.798 14.524 1.00 13.14 ATOM 2365 O GLN A 827 6.428 −16.23514.906 1.00 13.21 ATOM 2366 N LEU A 828 7.966 −14.596 14.862 1.00 10.02ATOM 2367 CA LEU A 828 7.182 −13.713 15.720 1.00 10.78 ATOM 2368 CB LEUA 828 8.037 −12.521 16.166 1.00 9.67 ATOM 2369 CG LEU A 828 7.315−11.431 16.966 1.00 14.41 ATOM 2370 CD1 LEU A 828 6.653 −12.048 18.1851.00 16.13 ATOM 2371 CD2 LEU A 828 8.300 −10.351 17.389 1.00 14.03 ATOM2372 C LEU A 828 5.902 −13.218 15.036 1.00 11.55 ATOM 2373 O LEU A 8284.814 −13.290 15.609 1.00 12.50 ATOM 2374 N TYR A 829 6.024 −12.71713.812 1.00 10.38 ATOM 2375 CA TYR A 829 4.851 −12.217 13.109 1.00 11.38ATOM 2376 CB TYR A 829 5.286 −11.392 11.892 1.00 9.07 ATOM 2377 CG TYR A829 5.967 −10.112 12.324 1.00 13.32 ATOM 2378 CD1 TYR A 829 5.298 −9.18913.118 1.00 8.62 ATOM 2379 CE1 TYR A 829 5.926 −8.037 13.569 1.00 10.58ATOM 2380 CD2 TYR A 829 7.290 −9.849 11.989 1.00 10.78 ATOM 2381 CE2 TYRA 829 7.930 −8.699 12.440 1.00 8.02 ATOM 2382 CZ TYR A 829 7.241 −7.80013.228 1.00 8.64 ATOM 2383 OH TYR A 829 7.867 −6.659 13.688 1.00 10.63ATOM 2384 C TYR A 829 3.908 −13.349 12.731 1.00 12.07 ATOM 2385 O TYR A829 2.704 −13.140 12.594 1.00 14.07 ATOM 2386 N GLU A 830 4.452 −14.55512.585 1.00 14.19 ATOM 2387 CA GLU A 830 3.614 −15.709 12.274 1.00 14.53ATOM 2388 CB GLU A 830 4.469 −16.919 11.881 1.00 15.21 ATOM 2389 CG GLUA 830 5.196 −16.751 10.557 1.00 18.48 ATOM 2390 CD GLU A 830 6.057−17.948 10.208 1.00 27.35 ATOM 2391 OE1 GLU A 830 6.422 −18.701 11.1331.00 25.55 ATOM 2392 OE2 GLU A 830 6.380 −18.127 9.014 1.00 25.64 ATOM2393 C GLU A 830 2.806 −16.027 13.531 1.00 15.34 ATOM 2394 O GLU A 8301.594 −16.245 13.462 1.00 15.05 ATOM 2395 N ALA A 831 3.484 −16.03714.679 1.00 12.88 ATOM 2396 CA ALA A 831 2.836 −16.319 15.958 1.00 13.60ATOM 2397 CB ALA A 831 3.877 −16.341 17.080 1.00 14.75 ATOM 2398 C ALA A831 1.764 −15.279 16.264 1.00 14.36 ATOM 2399 O ALA A 831 0.666 −15.61716.714 1.00 13.70 ATOM 2400 N LEU A 832 2.085 −14.010 16.026 1.00 11.70ATOM 2401 CA LEU A 832 1.135 −12.935 16.276 1.00 12.90 ATOM 2402 CB LEUA 832 1.800 −11.577 16.030 1.00 12.02 ATOM 2403 CG LEU A 832 0.935−10.334 16.256 1.00 13.07 ATOM 2404 CD1 LEU A 832 0.367 −10.354 17.6701.00 16.97 ATOM 2405 CD2 LEU A 832 1.764 −9.076 16.018 1.00 12.70 ATOM2406 C LEU A 832 −0.093 −13.098 15.382 1.00 13.07 ATOM 2407 O LEU A 832−1.221 −12.851 15.811 1.00 12.63 ATOM 2408 N THR A 833 0.125 −13.52214.140 1.00 10.33 ATOM 2409 CA THR A 833 −0.985 −13.720 13.213 1.0011.65 ATOM 2410 CB THR A 833 −0.471 −14.019 11.798 1.00 15.54 ATOM 2411OG1 THR A 833 0.250 −12.881 11.309 1.00 13.44 ATOM 2412 CG2 THR A 833−1.631 −14.319 10.856 1.00 20.09 ATOM 2413 C THR A 833 −1.856 −14.87513.709 1.00 13.24 ATOM 2414 O THR A 833 −3.070 −14.879 13.512 1.00 14.62ATOM 2415 N HIS A 834 −1.233 −15.855 14.358 1.00 12.04 ATOM 2416 CA HISA 834 −1.974 −16.988 14.901 1.00 15.35 ATOM 2417 CB HIS A 834 −1.010−18.045 15.451 1.00 17.31 ATOM 2418 CG HIS A 834 −1.686 −19.161 16.1741.00 21.70 ATOM 2419 CD2 HIS A 834 −2.005 −20.422 15.792 1.00 27.35 ATOM2420 ND1 HIS A 834 −2.158 −19.040 17.471 1.00 27.23 ATOM 2421 CE1 HIS A834 −2.728 −20.162 17.843 1.00 22.73 ATOM 2422 NE2 HIS A 834 −2.650−21.026 16.836 1.00 26.03 ATOM 2423 C HIS A 834 −2.907 −16.495 16.0111.00 16.43 ATOM 2424 O HIS A 834 −4.061 −16.917 16.101 1.00 16.32 ATOM2425 N VAL A 835 −2.402 −15.600 16.852 1.00 14.39 ATOM 2426 CA VAL A 835−3.201 −15.042 17.940 1.00 16.17 ATOM 2427 CB VAL A 835 −2.329 −14.17718.879 1.00 20.06 ATOM 2428 CG1 VAL A 835 −3.203 −13.433 19.878 1.0026.18 ATOM 2429 CG2 VAL A 835 −1.336 −15.067 19.616 1.00 22.85 ATOM 2430C VAL A 835 −4.345 −14.196 17.376 1.00 18.30 ATOM 2431 O VAL A 835−5.462 −14.219 17.899 1.00 16.68 ATOM 2432 N SER A 836 −4.061 −13.46116.302 1.00 15.55 ATOM 2433 CA SER A 836 −5.060 −12.620 15.646 1.0015.62 ATOM 2434 CB SER A 836 −5.081 −11.222 16.267 1.00 18.44 ATOM 2435OG SER A 836 −6.092 −10.430 15.665 1.00 24.05 ATOM 2436 C SER A 836−4.744 −12.516 14.153 1.00 15.03 ATOM 2437 O SER A 836 −3.754 −11.90113.759 1.00 14.82 ATOM 2438 N GLU A 837 −5.596 −13.123 13.334 1.00 16.29ATOM 2439 CA GLU A 837 −5.423 −13.139 11.886 1.00 16.40 ATOM 2440 CB GLUA 837 −6.578 −13.922 11.244 1.00 19.29 ATOM 2441 CG GLU A 837 −6.524−14.017 9.722 1.00 30.56 ATOM 2442 CD GLU A 837 −5.259 −14.685 9.2131.00 40.78 ATOM 2443 OE1 GLU A 837 −4.925 −15.785 9.704 1.00 33.63 ATOM2444 OE2 GLU A 837 −4.603 −14.112 8.316 1.00 45.55 ATOM 2445 C GLU A 837−5.324 −11.749 11.256 1.00 14.00 ATOM 2446 O GLU A 837 −4.672 −11.57410.227 1.00 16.56 ATOM 2447 N ASP A 838 −5.967 −10.762 11.871 1.00 14.38ATOM 2448 CA ASP A 838 −5.938 −9.402 11.349 1.00 12.78 ATOM 2449 CB ASPA 838 −6.990 −8.547 12.060 1.00 12.80 ATOM 2450 CG ASP A 838 −8.410−8.929 11.669 1.00 31.66 ATOM 2451 OD1 ASP A 838 −8.770 −8.750 10.4871.00 25.15 ATOM 2452 OD2 ASP A 838 −9.162 −9.414 12.540 1.00 29.94 ATOM2453 C ASP A 838 −4.558 −8.751 11.468 1.00 11.81 ATOM 2454 O ASP A 838−4.355 −7.625 11.017 1.00 12.87 ATOM 2455 N CYS A 839 −3.610 −9.45612.080 1.00 14.34 ATOM 2456 CA CYS A 839 −2.254 −8.929 12.203 1.00 14.23ATOM 2457 CB CYS A 839 −1.619 −9.354 13.533 1.00 12.27 ATOM 2458 SG CYSA 839 −2.115 −8.349 14.969 1.00 12.53 ATOM 2459 C CYS A 839 −1.412−9.440 11.038 1.00 15.74 ATOM 2460 O CYS A 839 −0.222 −9.142 10.941 1.0013.52 ATOM 2461 N PHE A 840 −2.044 −10.209 10.152 1.00 14.15 ATOM 2462CA PHE A 840 −1.364 −10.765 8.983 1.00 14.85 ATOM 2463 CB PHE A 840−2.370 −11.451 8.052 1.00 18.01 ATOM 2464 CG PHE A 840 −1.760 −11.9266.764 1.00 16.92 ATOM 2465 CD1 PHE A 840 −0.886 −13.001 6.751 1.00 13.52ATOM 2466 CD2 PHE A 840 −2.010 −11.257 5.575 1.00 19.38 ATOM 2467 CE1PHE A 840 −0.269 −13.398 5.575 1.00 23.30 ATOM 2468 CE2 PHE A 840 −1.397−11.649 4.396 1.00 23.75 ATOM 2469 CZ PHE A 840 −0.525 −12.720 4.3971.00 22.76 ATOM 2470 C PHE A 840 −0.541 −9.768 8.155 1.00 13.70 ATOM2471 O PHE A 840 0.546 −10.105 7.678 1.00 13.33 ATOM 2472 N PRO A 841−1.049 −8.537 7.958 1.00 12.97 ATOM 2473 CD PRO A 841 −2.369 −8.0028.339 1.00 14.47 ATOM 2474 CA PRO A 841 −0.294 −7.557 7.168 1.00 12.84ATOM 2475 CB PRO A 841 −1.127 −6.287 7.312 1.00 14.37 ATOM 2476 CG PRO A841 −2.533 −6.826 7.391 1.00 14.58 ATOM 2477 C PRO A 841 1.151 −7.3677.630 1.00 14.54 ATOM 2478 O PRO A 841 2.034 −7.065 6.826 1.00 13.75ATOM 2479 N LEU A 842 1.393 −7.530 8.926 1.00 11.66 ATOM 2480 CA LEU A842 2.747 −7.384 9.444 1.00 12.35 ATOM 2481 CB LEU A 842 2.732 −7.43010.977 1.00 11.85 ATOM 2482 CG LEU A 842 2.039 −6.228 11.624 1.00 12.78ATOM 2483 CD1 LEU A 842 1.900 −6.434 13.131 1.00 14.23 ATOM 2484 CD2 LEUA 842 2.837 −4.975 11.321 1.00 14.25 ATOM 2485 C LEU A 842 3.613 −8.5138.880 1.00 13.95 ATOM 2486 O LEU A 842 4.741 −8.290 8.444 1.00 13.84ATOM 2487 N LEU A 843 3.067 −9.727 8.882 1.00 11.90 ATOM 2488 CA LEU A843 3.779 −10.889 8.359 1.00 11.64 ATOM 2489 CB LEU A 843 2.995 −12.1618.670 1.00 10.07 ATOM 2490 CG LEU A 843 3.532 −13.468 8.084 1.00 9.50ATOM 2491 CD1 LEU A 843 4.940 −13.735 8.588 1.00 13.64 ATOM 2492 CD2 LEUA 843 2.597 −14.608 8.466 1.00 12.37 ATOM 2493 C LEU A 843 3.971 −10.7516.847 1.00 11.74 ATOM 2494 O LEU A 843 5.054 −11.003 6.319 1.00 13.14ATOM 2495 N ASP A 844 2.909 −10.342 6.160 1.00 13.31 ATOM 2496 CA ASP A844 2.943 −10.154 4.711 1.00 14.45 ATOM 2497 CB ASP A 844 1.573 −9.6394.245 1.00 18.19 ATOM 2498 CG ASP A 844 1.354 −9.771 2.739 1.00 13.51ATOM 2499 OD1 ASP A 844 2.141 −10.459 2.057 1.00 18.86 ATOM 2500 OD2 ASPA 844 0.367 −9.187 2.243 1.00 17.91 ATOM 2501 C ASP A 844 4.053 −9.1534.366 1.00 13.87 ATOM 2502 O ASP A 844 4.854 −9.386 3.460 1.00 13.07ATOM 2503 N GLY A 845 4.100 −8.046 5.104 1.00 12.67 ATOM 2504 CA GLY A845 5.115 −7.035 4.862 1.00 11.69 ATOM 2505 C GLY A 845 6.529 −7.5405.097 1.00 11.05 ATOM 2506 O GLY A 845 7.447 −7.240 4.330 1.00 12.51ATOM 2507 N CYS A 846 6.704 −8.314 6.161 1.00 10.28 ATOM 2508 CA CYS A846 8.005 −8.882 6.507 1.00 10.93 ATOM 2509 CB CYS A 846 7.889 −9.6437.831 1.00 14.58 ATOM 2510 SG CYS A 846 9.443 −10.273 8.485 1.00 12.82ATOM 2511 C CYS A 846 8.497 −9.821 5.398 1.00 11.92 ATOM 2512 O CYS A846 9.661 −9.762 4.985 1.00 11.24 ATOM 2513 N ARG A 847 7.605 −10.6834.914 1.00 12.77 ATOM 2514 CA ARG A 847 7.953 −11.618 3.853 1.00 13.72ATOM 2515 CB ARG A 847 6.762 −12.527 3.535 1.00 11.63 ATOM 2516 CG ARG A847 6.457 −13.545 4.619 1.00 13.10 ATOM 2517 CD ARG A 847 5.180 −14.3084.316 1.00 17.35 ATOM 2518 NE ARG A 847 4.978 −15.402 5.262 1.00 19.23ATOM 2519 CZ ARG A 847 3.840 −16.077 5.389 1.00 21.47 ATOM 2520 NH1 ARGA 847 2.796 −15.769 4.632 1.00 24.29 ATOM 2521 NH2 ARG A 847 3.750−17.059 6.275 1.00 27.21 ATOM 2522 C ARG A 847 8.371 −10.870 2.592 1.0013.53 ATOM 2523 O ARG A 847 9.320 −11.265 1.906 1.00 13.20 ATOM 2524 NLYS A 848 7.659 −9.793 2.283 1.00 12.35 ATOM 2525 CA LYS A 848 7.977−9.007 1.099 1.00 14.65 ATOM 2526 CB LYS A 848 6.925 −7.915 0.880 1.0016.22 ATOM 2527 CG LYS A 848 5.567 −8.447 0.413 1.00 14.77 ATOM 2528 CDLYS A 848 4.579 −7.308 0.195 1.00 19.65 ATOM 2529 CE LYS A 848 3.210−7.817 −0.206 1.00 19.42 ATOM 2530 NZ LYS A 848 2.214 −6.709 −0.212 1.0023.11 ATOM 2531 C LYS A 848 9.364 −8.392 1.229 1.00 14.80 ATOM 2532 OLYS A 848 10.112 −8.319 0.253 1.00 13.12 ATOM 2533 N ASN A 849 9.713−7.953 2.435 1.00 13.42 ATOM 2534 CA ASN A 849 11.034 −7.369 2.648 1.0013.07 ATOM 2535 CB ASN A 849 11.086 −6.646 3.995 1.00 13.67 ATOM 2536 CGASN A 849 10.412 −5.288 3.950 1.00 17.85 ATOM 2537 OD1 ASN A 849 9.863−4.821 4.949 1.00 16.87 ATOM 2538 ND2 ASN A 849 10.461 −4.638 2.790 1.0013.21 ATOM 2539 C ASN A 849 12.122 −8.434 2.568 1.00 12.00 ATOM 2540 OASN A 849 13.252 −8.148 2.165 1.00 11.88 ATOM 2541 N ARG A 850 11.797−9.667 2.945 1.00 11.53 ATOM 2542 CA ARG A 850 12.793 −10.729 2.860 1.0011.98 ATOM 2543 CB ARG A 850 12.285 −12.037 3.473 1.00 14.13 ATOM 2544CG ARG A 850 13.373 −13.110 3.508 1.00 13.55 ATOM 2545 CD ARG A 85012.838 −14.511 3.781 1.00 18.02 ATOM 2546 NE ARG A 850 13.930 −15.4574.001 1.00 16.95 ATOM 2547 CZ ARG A 850 14.743 −15.919 3.052 1.00 14.40ATOM 2548 NH1 ARG A 850 14.595 −15.533 1.790 1.00 16.03 ATOM 2549 NH2ARG A 850 15.727 −16.754 3.373 1.00 12.51 ATOM 2550 C ARG A 850 13.138−10.972 1.399 1.00 13.81 ATOM 2551 O ARG A 850 14.304 −11.151 1.054 1.0015.14 ATOM 2552 N GLN A 851 12.118 −10.985 0.542 1.00 16.03 ATOM 2553 CAGLN A 851 12.317 −11.193 −0.892 1.00 15.42 ATOM 2554 CB GLN A 851 10.969−11.156 −1.622 1.00 17.30 ATOM 2555 CG GLN A 851 11.039 −11.399 −3.1271.00 30.46 ATOM 2556 CD GLN A 851 11.475 −10.174 −3.912 1.00 34.81 ATOM2557 OE1 GLN A 851 10.862 −9.110 −3.814 1.00 37.41 ATOM 2558 NE2 GLN A851 12.534 −10.320 −4.704 1.00 40.89 ATOM 2559 C GLN A 851 13.229−10.109 −1.436 1.00 16.49 ATOM 2560 O GLN A 851 14.151 −10.371 −2.2081.00 15.70 ATOM 2561 N LYS A 852 12.953 −8.867 −1.014 1.00 15.86 ATOM2562 CA LYS A 852 13.705 −7.685 −1.428 1.00 16.63 ATOM 2563 CB LYS A 85213.065 −6.405 −0.838 1.00 13.58 ATOM 2564 CG LYS A 852 11.802 −6.008−1.561 1.00 18.37 ATOM 2565 CD LYS A 852 12.183 −5.582 −2.958 1.00 31.95ATOM 2566 CE LYS A 852 11.002 −5.087 −3.751 1.00 37.83 ATOM 2567 NZ LYSA 852 11.421 −4.599 −5.099 1.00 41.92 ATOM 2568 C LYS A 852 15.175−7.754 −1.037 1.00 15.46 ATOM 2569 O LYS A 852 16.055 −7.542 −1.874 1.0014.58 ATOM 2570 N TRP A 853 15.446 −8.063 0.225 1.00 12.99 ATOM 2571 CATRP A 853 16.821 −8.168 0.705 1.00 12.72 ATOM 2572 CB TRP A 853 16.843−8.299 2.228 1.00 11.94 ATOM 2573 CG TRP A 853 16.640 −7.011 2.957 1.0011.40 ATOM 2574 CD2 TRP A 853 17.485 −5.864 2.913 1.00 14.74 ATOM 2575CE2 TRP A 853 16.929 −4.888 3.763 1.00 12.41 ATOM 2576 CE3 TRP A 85318.675 −5.554 2.236 1.00 10.90 ATOM 2577 CD1 TRP A 853 15.618 −6.7013.813 1.00 11.02 ATOM 2578 NE1 TRP A 853 15.781 −5.429 4.303 1.00 14.15ATOM 2579 CZ2 TRP A 853 17.502 −3.638 3.958 1.00 12.03 ATOM 2580 CZ3 TRPA 853 19.246 −4.312 2.427 1.00 13.77 ATOM 2581 CH2 TRP A 853 18.663−3.370 3.280 1.00 16.08 ATOM 2582 C TRP A 853 17.543 −9.357 0.074 1.0013.55 ATOM 2583 O TRP A 853 18.722 −9.265 −0.282 1.00 13.19 ATOM 2584 NGLN A 854 16.836 −10.472 −0.062 1.00 12.06 ATOM 2585 CA GLN A 854 17.427−11.667 −0.657 1.00 13.49 ATOM 2586 CB GLN A 854 16.426 −12.822 −0.6301.00 13.86 ATOM 2587 CG GLN A 854 16.934 −14.128 −1.242 1.00 15.91 ATOM2588 CD GLN A 854 18.267 −14.585 −0.665 1.00 23.66 ATOM 2589 OE1 GLN A854 18.544 −14.404 0.520 1.00 20.44 ATOM 2590 NE2 GLN A 854 19.091−15.199 −1.504 1.00 26.84 ATOM 2591 C GLN A 854 17.869 −11.400 −2.0941.00 13.14 ATOM 2592 O GLN A 854 18.920 −11.880 −2.524 1.00 15.55 ATOM2593 N ALA A 855 17.069 −10.635 −2.832 1.00 14.63 ATOM 2594 CA ALA A 85517.408 −10.318 −4.219 1.00 15.08 ATOM 2595 CB ALA A 855 16.264 −9.563−4.884 1.00 17.06 ATOM 2596 C ALA A 855 18.697 −9.504 −4.303 1.00 16.23ATOM 2597 O ALA A 855 19.439 −9.611 −5.278 1.00 17.06 ATOM 2598 N LEU A856 18.959 −8.689 −3.287 1.00 15.11 ATOM 2599 CA LEU A 856 20.178 −7.889−3.261 1.00 17.23 ATOM 2600 CB LEU A 856 20.031 −6.715 −2.284 1.00 11.53ATOM 2601 CG LEU A 856 18.968 −5.676 −2.643 1.00 15.60 ATOM 2602 CD1 LEUA 856 18.996 −4.549 −1.634 1.00 19.73 ATOM 2603 CD2 LEU A 856 19.226−5.145 −4.047 1.00 12.95 ATOM 2604 C LEU A 856 21.362 −8.754 −2.835 1.0017.35 ATOM 2605 O LEU A 856 22.478 −8.601 −3.337 1.00 17.30 ATOM 2606 NALA A 857 21.109 −9.674 −1.911 1.00 16.52 ATOM 2607 CA ALA A 857 22.156−10.545 −1.396 1.00 17.82 ATOM 2608 CB ALA A 857 21.708 −11.155 −0.0791.00 15.78 ATOM 2609 C ALA A 857 22.616 −11.651 −2.339 1.00 19.95 ATOM2610 O ALA A 857 23.781 −12.048 −2.305 1.00 21.30 ATOM 2611 N GLU A 85821.715 −12.144 −3.181 1.00 19.75 ATOM 2612 CA GLU A 858 22.059 −13.233−4.091 1.00 23.14 ATOM 2613 CB GLU A 858 20.798 −14.008 −4.475 1.0028.23 ATOM 2614 CG GLU A 858 19.735 −13.155 −5.139 1.00 35.46 ATOM 2615CD GLU A 858 18.516 −13.957 −5.548 1.00 41.30 ATOM 2616 OE1 GLU A 85817.928 −14.635 −4.679 1.00 46.06 ATOM 2617 OE2 GLU A 858 18.144 −13.905−6.739 1.00 53.40 ATOM 2618 C GLU A 858 22.773 −12.775 −5.356 1.00 24.66ATOM 2619 O GLU A 858 22.769 −11.561 −5.640 1.00 27.06 ATOM 2620 OXT GLUA 858 23.319 −13.654 −6.053 1.00 33.90 TER 2621 GLU A 858 ATOM 2622 OHOH W 1 14.659 12.373 18.930 1.00 11.90 ATOM 2623 O HOH W 2 9.029 0.61615.467 1.00 15.60 ATOM 2624 O HOH W 3 17.339 −0.310 24.269 1.00 9.87ATOM 2625 O HOH W 4 17.787 8.492 22.312 1.00 9.91 ATOM 2626 O HOH W 522.322 0.101 41.405 1.00 10.58 ATOM 2627 O HOH W 6 7.037 −4.929 2.9381.00 15.52 ATOM 2628 O HOH W 7 24.844 0.942 17.890 1.00 12.19 ATOM 2629O HOH W 8 17.812 −5.285 21.940 1.00 13.09 ATOM 2630 O HOH W 9 19.355−1.244 21.749 1.00 11.09 ATOM 2631 O HOH W 10 11.998 −15.929 13.123 1.0015.08 ATOM 2632 O HOH W 11 17.595 6.868 5.858 1.00 17.40 ATOM 2633 O HOHW 12 20.522 −8.124 28.490 1.00 16.30 ATOM 2634 O HOH W 13 7.122 8.42630.706 1.00 12.74 ATOM 2635 O HOH W 14 14.281 −0.736 24.882 1.00 10.20ATOM 2636 O HOH W 15 27.778 −4.812 7.714 1.00 14.34 ATOM 2637 O HOH W 1645.697 −5.856 19.373 1.00 13.79 ATOM 2638 O HOH W 17 32.028 0.851 11.8591.00 12.49 ATOM 2639 O HOH W 18 12.716 −7.833 22.260 1.00 11.62 ATOM2640 O HOH W 19 20.770 −7.019 24.953 1.00 13.66 ATOM 2641 O HOH W 209.679 −8.387 30.457 1.00 18.04 ATOM 2642 O HOH W 21 20.996 −1.566 19.5841.00 15.27 ATOM 2643 O HOH W 22 5.367 −8.570 29.548 1.00 17.36 ATOM 2644O HOH W 23 25.138 −9.337 1.725 1.00 17.63 ATOM 2645 O HOH W 24 −9.020−0.116 43.708 1.00 15.91 ATOM 2646 O HOH W 25 22.657 −6.174 29.194 1.0017.18 ATOM 2647 O HOH W 26 −4.280 19.557 21.192 1.00 19.85 ATOM 2648 OHOH W 27 14.289 6.604 13.852 1.00 14.85 ATOM 2649 O HOH W 28 11.411−1.302 13.935 1.00 12.80 ATOM 2650 O HOH W 29 11.700 13.882 15.200 1.0014.97 ATOM 2651 O HOH W 30 18.410 10.076 12.196 1.00 19.59 ATOM 2652 OHOH W 31 26.709 7.571 23.378 1.00 17.44 ATOM 2653 O HOH W 32 25.4205.805 17.773 1.00 17.40 ATOM 2654 O HOH W 33 11.087 10.589 10.070 1.0017.81 ATOM 2655 O HOH W 34 11.500 −19.954 26.231 1.00 16.07 ATOM 2656 OHOH W 35 −5.204 −5.042 34.106 1.00 17.24 ATOM 2657 O HOH W 36 1.9419.940 36.428 1.00 13.95 ATOM 2658 O HOH W 37 23.916 7.238 15.924 1.0014.00 ATOM 2659 O HOH W 38 4.522 21.473 19.911 1.00 20.60 ATOM 2660 OHOH W 39 7.654 32.374 24.586 1.00 19.77 ATOM 2661 O HOH W 40 −11.1058.617 12.732 1.00 20.19 ATOM 2662 O HOH W 41 14.266 14.289 20.855 1.0016.50 ATOM 2663 O HOH W 42 27.797 −9.140 13.072 1.00 17.28 ATOM 2664 OHOH W 43 13.361 −5.781 20.636 1.00 17.62 ATOM 2665 O HOH W 44 9.43917.952 22.920 1.00 20.34 ATOM 2666 O HOH W 45 13.506 −19.339 23.851 1.0017.51 ATOM 2667 O HOH W 46 −9.608 −2.484 44.794 1.00 18.03 ATOM 2668 OHOH W 47 19.179 −3.517 23.479 1.00 14.63 ATOM 2669 O HOH W 48 20.825−1.771 7.357 1.00 15.56 ATOM 2670 O HOH W 49 3.953 −2.401 8.103 1.0015.98 ATOM 2671 O HOH W 50 5.164 2.828 12.389 1.00 17.57 ATOM 2672 O HOHW 51 22.475 −6.004 8.390 1.00 20.31 ATOM 2673 O HOH W 52 −1.505 −7.7133.922 1.00 20.93 ATOM 2674 O HOH W 53 16.030 13.344 15.066 1.00 22.86ATOM 2675 O HOH W 54 3.120 33.114 17.327 1.00 18.81 ATOM 2676 O HOH W 556.517 19.676 19.112 1.00 20.43 ATOM 2677 O HOH W 56 27.812 5.941 11.2691.00 19.39 ATOM 2678 O HOH W 57 14.704 9.138 12.638 1.00 17.37 ATOM 2679O HOH W 58 10.813 −19.129 28.734 1.00 23.50 ATOM 2680 O HOH W 59 9.603−13.958 1.403 1.00 20.05 ATOM 2681 O HOH W 60 46.209 −3.550 17.835 1.0018.22 ATOM 2682 O HOH W 61 24.760 −2.396 10.006 1.00 20.80 ATOM 2683 OHOH W 62 11.077 3.087 12.585 1.00 21.05 ATOM 2684 O HOH W 63 10.534−10.726 28.998 1.00 21.18 ATOM 2685 O HOH W 64 −0.961 −11.064 33.4401.00 18.63 ATOM 2686 O HOH W 65 20.890 0.577 15.388 1.00 19.77 ATOM 2687O HOH W 66 21.685 13.866 20.281 1.00 24.54 ATOM 2688 O HOH W 67 −5.012−3.878 8.180 1.00 21.24 ATOM 2689 O HOH W 68 −10.443 9.371 15.194 1.0019.03 ATOM 2690 O HOH W 69 26.635 8.578 39.152 1.00 19.48 ATOM 2691 OHOH W 70 21.837 −4.044 23.094 1.00 14.46 ATOM 2692 O HOH W 71 18.9790.534 3.275 1.00 19.32 ATOM 2693 O HOH W 72 −7.687 −4.529 35.484 1.0019.76 ATOM 2694 O HOH W 73 −4.441 9.972 35.483 1.00 21.75 ATOM 2695 OHOH W 74 22.147 0.611 18.233 1.00 21.06 ATOM 2696 O HOH W 75 25.6257.694 19.834 1.00 17.79 ATOM 2697 O HOH W 76 −9.716 14.941 11.027 1.0020.22 ATOM 2698 O HOH W 77 14.015 −1.710 16.866 1.00 19.03 ATOM 2699 OHOH W 78 21.861 −3.953 20.354 1.00 17.68 ATOM 2700 O HOH W 79 21.854−11.471 10.659 1.00 21.05 ATOM 2701 O HOH W 80 15.795 −5.944 −4.295 1.0017.34 ATOM 2702 O HOH W 81 26.427 −5.333 20.748 1.00 28.65 ATOM 2703 OHOH W 82 0.806 16.637 36.547 1.00 22.11 ATOM 2704 O HOH W 83 28.8835.909 33.300 1.00 35.99 ATOM 2705 O HOH W 84 0.615 −5.836 36.804 1.0021.63 ATOM 2706 O HOH W 85 14.416 −12.696 −3.692 1.00 22.36 ATOM 2707 OHOH W 86 −4.841 7.644 43.980 1.00 19.92 ATOM 2708 O HOH W 87 −6.0595.564 10.293 1.00 22.49 ATOM 2709 O HOH W 88 7.210 1.031 13.002 1.0019.78 ATOM 2710 O HOH W 89 −5.786 −6.329 9.023 1.00 20.32 ATOM 2711 OHOH W 90 19.117 4.909 35.027 1.00 17.30 ATOM 2712 O HOH W 91 10.59213.017 38.293 1.00 23.66 ATOM 2713 O HOH W 92 −9.801 5.234 16.132 1.0020.64 ATOM 2714 O HOH W 93 −6.370 −17.172 24.540 1.00 23.65 ATOM 2715 OHOH W 94 −6.833 1.342 45.207 1.00 17.92 ATOM 2716 O HOH W 95 33.715−7.279 11.000 1.00 17.67 ATOM 2717 O HOH W 96 5.722 31.659 29.252 1.0019.35 ATOM 2718 O HOH W 97 14.155 −2.890 10.083 1.00 16.30 ATOM 2719 OHOH W 98 19.709 −5.898 20.414 1.00 27.45 ATOM 2720 O HOH W 99 4.418−3.958 2.629 1.00 23.70 ATOM 2721 O HOH W 100 5.739 5.419 41.566 1.0026.30 ATOM 2722 O HOH W 101 1.882 −10.334 12.547 1.00 21.56 ATOM 2723 OHOH W 102 1.506 9.558 7.516 1.00 21.76 ATOM 2724 O HOH W 103 23.2111.757 4.698 1.00 23.21 ATOM 2725 O HOH W 104 36.282 2.363 9.440 1.0027.13 ATOM 2726 O HOH W 105 27.600 −11.267 2.472 1.00 18.59 ATOM 2727 OHOH W 106 16.305 16.757 22.862 1.00 25.14 ATOM 2728 O HOH W 107 21.223−0.443 4.807 1.00 20.51 ATOM 2729 O HOH W 108 12.939 13.840 12.680 1.0026.10 ATOM 2730 O HOH W 109 10.191 −9.652 24.549 1.00 17.97 ATOM 2731 OHOH W 110 9.527 −19.990 11.160 1.00 34.52 ATOM 2732 O HOH W 111 2.300−4.117 6.982 1.00 21.40 ATOM 2733 O HOH W 112 31.807 5.599 25.384 1.0019.28 ATOM 2734 O HOH W 113 11.858 5.625 12.858 1.00 18.80 ATOM 2735 OHOH W 114 2.975 3.851 3.583 1.00 28.02 ATOM 2736 O HOH W 115 22.328−3.325 9.278 1.00 18.13 ATOM 2737 O HOH W 116 7.581 21.278 17.210 1.0026.33 ATOM 2738 O HOH W 117 −8.959 18.330 19.702 1.00 25.41 ATOM 2739 OHOH W 118 −7.913 −3.625 46.688 1.00 16.16 ATOM 2740 O HOH W 119 29.369−4.122 35.016 1.00 21.35 ATOM 2741 O HOH W 120 −10.313 4.301 39.676 1.0020.84 ATOM 2742 O HOH W 121 36.288 −8.163 10.383 1.00 29.41 ATOM 2743 OHOH W 122 −5.305 0.154 7.066 1.00 32.03 ATOM 2744 O HOH W 123 15.8929.345 6.948 1.00 31.98 ATOM 2745 O HOH W 124 −7.934 −11.981 26.594 1.0024.88 ATOM 2746 O HOH W 125 −7.700 −14.762 14.417 1.00 27.16 ATOM 2747 OHOH W 126 7.924 19.345 32.073 1.00 27.10 ATOM 2748 O HOH W 127 22.963−15.271 −0.194 1.00 34.57 ATOM 2749 O HOH W 128 14.018 4.418 0.344 1.0027.94 ATOM 2750 O HOH W 129 13.334 16.377 17.301 1.00 27.05 ATOM 2751 OHOH W 130 30.641 −11.391 0.176 1.00 21.79 ATOM 2752 O HOH W 131 −5.143−9.116 6.397 1.00 26.22 ATOM 2753 O HOH W 132 44.452 2.118 22.189 1.0025.35 ATOM 2754 O HOH W 133 −0.942 −8.268 32.526 1.00 21.73 ATOM 2755 OHOH W 134 32.286 8.100 17.531 1.00 30.18 ATOM 2756 O HOH W 135 4.471−22.268 17.254 1.00 22.18 ATOM 2757 O HOH W 136 20.964 −7.154 10.0511.00 23.34 ATOM 2758 O HOH W 137 −6.984 26.107 22.746 1.00 26.33 ATOM2759 O HOH W 138 17.856 14.348 24.807 1.00 20.33 ATOM 2760 O HOH W 13910.038 −5.546 41.193 1.00 26.62 ATOM 2761 O HOH W 140 13.989 13.83716.687 1.00 27.53 ATOM 2762 O HOH W 141 23.629 −13.084 9.502 1.00 28.21ATOM 2763 O HOH W 142 31.635 7.713 14.307 1.00 30.30 ATOM 2764 O HOH W143 6.811 −2.344 −0.868 1.00 24.47 ATOM 2765 O HOH W 144 7.278 −9.98130.756 1.00 27.03 ATOM 2766 O HOH W 145 −6.981 7.089 6.281 1.00 26.94ATOM 2767 O HOH W 146 −8.635 18.558 29.861 1.00 27.91 ATOM 2768 O HOH W147 30.525 −1.680 34.334 1.00 24.09 ATOM 2769 O HOH W 148 2.251 −13.8672.121 1.00 25.49 ATOM 2770 O HOH W 149 −8.063 −9.740 29.191 1.00 24.34ATOM 2771 O HOH W 150 −1.333 15.279 37.020 1.00 28.81 ATOM 2772 O HOH W151 18.429 15.610 21.408 1.00 22.50 ATOM 2773 O HOH W 152 13.471 −4.26412.528 1.00 19.38 ATOM 2774 O HOH W 153 18.621 −17.600 7.222 1.00 21.52ATOM 2775 O HOH W 154 19.181 −5.396 13.023 1.00 33.83 ATOM 2776 O HOH W155 −3.698 −11.419 33.622 1.00 22.32 ATOM 2777 O HOH W 156 24.773 −7.68726.828 1.00 25.23 ATOM 2778 O HOH W 157 11.338 6.981 10.450 1.00 25.98ATOM 2779 O HOH W 158 7.187 4.097 9.722 1.00 25.73 ATOM 2780 O HOH W 15910.571 18.276 18.940 1.00 26.56 ATOM 2781 O HOH W 160 29.444 8.13818.655 1.00 25.10 ATOM 2782 O HOH W 161 −4.733 −16.782 12.321 1.00 23.51ATOM 2783 O HOH W 162 24.194 7.218 40.602 1.00 28.88 ATOM 2784 O HOH W163 13.925 −7.040 −5.961 1.00 29.58 ATOM 2785 O HOH W 164 −8.456 17.42510.469 1.00 25.03 ATOM 2786 O HOH W 165 20.283 7.809 6.109 1.00 25.58ATOM 2787 O HOH W 166 11.226 1.360 14.389 1.00 28.28 ATOM 2788 O HOH W167 17.600 11.985 25.766 1.00 28.21 ATOM 2789 O HOH W 168 −1.369 0.3646.150 1.00 26.61 ATOM 2790 O HOH W 169 1.250 6.912 6.112 1.00 22.96 ATOM2791 O HOH W 170 13.982 16.820 19.827 1.00 26.70 ATOM 2792 O HOH W 1718.401 6.117 8.285 1.00 29.37 ATOM 2793 O HOH W 172 1.561 32.980 20.3151.00 25.71 ATOM 2794 O HOH W 173 8.687 −4.960 0.724 1.00 20.63 ATOM 2795O HOH W 174 16.762 −8.584 32.541 1.00 22.53 ATOM 2796 O HOH W 175 −8.92823.790 25.122 1.00 26.68 ATOM 2797 O HOH W 176 30.774 −10.692 12.7811.00 29.33 ATOM 2798 O HOH W 177 −4.491 −0.583 48.435 1.00 27.59 ATOM2799 O HOH W 178 −10.254 8.887 25.677 1.00 27.41 ATOM 2800 O HOH W 17912.487 −14.347 0.366 1.00 29.02 ATOM 2801 O HOH W 180 −2.194 −3.1935.572 1.00 37.26 ATOM 2802 O HOH W 181 21.240 −14.747 4.723 1.00 24.12ATOM 2803 O HOH W 182 25.238 15.872 21.083 1.00 33.15 ATOM 2804 O HOH W183 27.650 8.541 12.497 1.00 23.15 ATOM 2805 O HOH W 184 35.303 3.83726.688 1.00 23.28 ATOM 2806 O HOH W 185 −3.730 14.555 34.107 1.00 23.34ATOM 2807 O HOH W 186 −8.927 −4.660 10.381 1.00 28.70 ATOM 2808 O HOH W187 40.695 −1.179 15.166 1.00 31.35 ATOM 2809 O HOH W 188 −0.356 −22.61531.607 1.00 35.28 ATOM 2810 O HOH W 189 3.463 34.674 22.382 1.00 27.20ATOM 2811 O HOH W 190 8.911 2.196 11.376 1.00 19.30 ATOM 2812 O HOH W191 −2.598 −24.115 28.861 1.00 26.04 ATOM 2813 O HOH W 192 8.418 −15.51034.179 1.00 38.02 ATOM 2814 O HOH W 193 15.703 −17.633 −0.060 1.00 35.88ATOM 2815 O HOH W 194 32.518 0.997 3.614 1.00 34.25 ATOM 2816 O HOH W195 19.062 −16.798 10.198 1.00 27.69 ATOM 2817 O HOH W 196 13.216 8.97610.392 1.00 27.61 ATOM 2818 O HOH W 197 2.647 −0.086 12.019 1.00 23.91ATOM 2819 O HOH W 198 −1.276 −7.561 35.325 1.00 25.96 ATOM 2820 O HOH W199 4.267 −22.362 30.170 1.00 35.68 ATOM 2821 O HOH W 200 21.787 10.59530.558 1.00 32.19 ATOM 2822 O HOH W 201 21.638 20.389 14.210 1.00 43.09ATOM 2823 O HOH W 202 5.373 −10.297 38.927 1.00 36.29 ATOM 2824 O HOH W203 29.035 −9.588 1.139 1.00 25.61 ATOM 2825 O HOH W 204 0.403 −17.62911.462 1.00 25.52 ATOM 2826 O HOH W 205 15.896 −2.824 23.429 1.00 9.81ATOM 2827 O HOH W 206 13.783 −1.283 21.923 1.00 12.03 ATOM 2828 O HOH W207 16.854 −0.738 21.328 1.00 11.76 ATOM 2829 O HOH W 208 14.946 −0.46519.263 1.00 10.55 ATOM 2830 O HOH W 209 −5.566 −9.500 29.835 1.00 34.12ATOM 2831 O HOH W 210 11.435 14.251 33.693 1.00 48.96 ATOM 2832 O HOH W211 3.944 31.281 18.816 1.00 43.83 ATOM 2833 O HOH W 212 21.511 8.20140.401 1.00 42.14 ATOM 2834 O HOH W 213 44.825 1.178 19.793 1.00 52.54ATOM 2835 O HOH W 214 9.397 20.244 23.958 1.00 30.91 ATOM 2836 O HOH W215 18.636 −1.182 15.865 1.00 23.82 ATOM 2837 O HOH W 216 18.955 −2.69317.957 1.00 28.82 ATOM 2838 O HOH W 217 26.248 −9.541 27.965 1.00 25.10ATOM 2839 O HOH W 218 24.703 −9.867 30.146 1.00 25.52 ATOM 2840 O HOH W219 22.600 −9.260 25.832 1.00 26.71 ATOM 2841 O HOH W 220 1.825 10.05439.457 1.00 25.12 ATOM 2842 O HOH W 221 3.585 4.590 45.058 1.00 28.59ATOM 2843 O HOH W 222 3.777 −6.424 30.447 1.00 24.42 TER 2844 HOH W 222ATOM 2845 ZN ZN B 864 13.210 0.069 20.406 1.00 15.15 ATOM 2846 MG MG B865 15.487 −0.725 23.006 1.00 8.84 TER 2847 MG B 865 END

REFERENCES

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[0219] Aravind, L. & Ponting, C. P. (1997) TIBS. 22, 458-459.

[0220] Brünger, A. et al. (1998), Acta Crystallogr. D 54, 905-921.

[0221] Butcher, R. W. & Sutherland, E. W. (1962) J. biol. Chem. 237,1244-1250.

[0222] Charbonneau, H. (1990) in Cyclic Nucleotide Phosphodiesterases:Structure, Regulation and Drug Action (Beavo, J., and Houslay, M. D.,eds) pp. 267-296, John Wiley & Sons, Inc., New York.

[0223] Charbonneau, H. et al., (1986) Proc. Natl. Acad. Sci. U. S. A.,83, 9308-9312.

[0224] Collaborative Computational Project Number 4 (1994) ActaCrystallogr. D 50, 760-763.

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[0226] de La Fortelle, E. & Bricogne, G. (1997) Methods Enzymol. 276,472-494.

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[0228] Goldberg, N. D. et al. (1980) J. Biol. Chem. 255, 10344-10347.

[0229] Hendrickson, W. A. et al. (1989) Basic Life Sci. 51 (SynchrotronRadiat. Struct. Biol.), 317-324.

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[0233] Martinez, S. et al. (2001) Poster presented at the AmericanCrystallography Association annual meeting, Los Angeles, USA.

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[0237] Quanta98, 1998, version 98.1111; Molecular Simulations Inc., SanDiego, Calif. 92121-3752.

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[0239] Soderling, S. H. & Beavo, J. A., (2000) Curr. Opin. Cell Biol.12, 174-179.

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[0241] Terwilliger, T. C. & Berendzen, J. (1997) Acta Crystallogr. D 53,571-579 Crystallogr. D 54, 799-804.

[0242] Thomas et al. (1990) J. Biol. Chem. 265, 14971-14978.

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[0244] J.Navaza, (1994) Acta Cryst. A50, 157-163.

Abbreviations

[0245] cAMP cyclic adenosine monophosphate cGMP cyclic guanosinemonophosphate PDE phosphodiesterase PGK protein kinase G MADmulti-wavelength anomalous dispersion PCR polymerase chain reaction 2YT16 g tryptone, 10 g yeast extract, 5 g NaCl per litre solution Tristris[hydroxymethyl]amino-methane E-64epoxysuccinyl-1-leucylamido-(4-guanidino) butane DTT DL-dithiothreitolβ-ME β-mercaptoethanol IPTG β-D-isopropyl-thiogalactopyranoside EDTAethylenediamine tetraacetic acid Bis-Trisbis[2-hydroxyethyl]imino-tris[hydroxymethyl]methane PEG polyethyleneglycol PEG2KMME polyethylene glycol 2000 monomethyl ether rmsd root meansquare deviation rpm revolutions per minute Moi multiplicity ofinfection Sildenafil5-[2-ethoxy-5-(4-methyl-1-piperazinylsulphonyl)phenyl]-1-methyl-3-n-propyl-1,6-dihydro-7H-pyrazolo[4,3-d] pyrimidin-7-one,which is also known as 1-[[3-(6,7-dihydro-1-methyl-7-oxo-3-propyl-1H-pyrazolo[4,3-d]pyrimidin-5-yl)-4-ethoxyphenyl]sulphonyl]-4- methylpiperazine (seeEP-A-0463756) UK-092,480 see “Sildenafil” UK-088,8005-(2-ethoxyphenyl)-1-methyl-3-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one.

List of Sequences

[0246] Wild-type PDE5 “loop region” HRGVNNSYIQRSEHPLAQLYCHSIME SEQ IDNO:1 Wild-type PDE5 catalytic domainEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNF SEQ ID NO:2QMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQWSGLSIEEYKTTLKIIKQAWATDLALYTKRRGEFFEURKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFTDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN Full length wild-type PDE5 sequenceERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATRE SEQ ID NO:3MVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIELHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCTRLEWNIKIGIVGHVAALGEPLNTKDAYEDPRFNAEVDQITGYKTQSILCMPTKNITREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLWEEQQSLEVILKKIAATHSFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKINYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNWPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAE QQEKMLTNGESGQAKRNWild-type PDE4 “loop region” HPGVSNQFLINTNSELALMYNDESVLE SEQ ID NO:4Loop-swapped PDE5 catalytic domain =PDE5 *EEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTTRMFTDLNLVQNF SEQ ID NO:5QMKHEVLCRWILSVKXNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHPGVSNQFLINTNSELALMYNDESVLEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKJPSMQVGFIDATCLQLYEALTHVSEDCFPLLDGCRKNRQKWQ ALAE Full lengthPDES sequence comprising PDE5 *ERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATRE SEQ ID NO:6MVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHWLHIHGLISADRYSLFLVCEDSSNPKFLISRLFDVAEGSTLEEVSNNCIIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLWEEQQSLEVILKKIAATIISFMQVQKCTWWDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHPGVSNQFLINTNSELALMYNDESVLEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYTKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNXIPSMQVGFIIDAICLQLYEALTHVSEDCFPLLDGCRRNRQKWQ ALAECGTGAATTCATGGAGGAAGAAACAAGAGAGCTAC SEQ ID NO:7CGTTCTAGACTATCAGTTCCGCTTGGCCTGGCCGCTTTCCCC SEQ ID NO:8CGTGAATTCATGCATCATCATCATCATCATCTTCTGGTTCCGCGTGGATCTG SEQ ID NO:9CGCCCGAGGAAGAAACAAGAGAGCTACCAAAGAAAGTTCTGAATTTGTGTTGATGAGAAACTGATTGGAGACTCCAG SEQ ID NO:10GATGATCCAAATCGTGGCTTAGATCAACACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTTG SEQ ID NO:11GAACACCATCATTTTGACCAG CGTTCTAGACTATCATTCTGCAAGGGCCTGCCATTTCTG SEQ IDNO:12 CGTCATATGGAGGAAGAAACAAGAGAGCTAC SEQ ID NO:13CGTCTCGAGCTATCATTCTGCAAGGGCCTGCCATTTCTG SEQ ID NO:14

[0247]

1 14 1 26 PRT Homo Sapiens 1 His Arg Gly Val Asn Asn Ser Tyr Ile Gln ArgSer Glu His Pro Leu 1 5 10 15 Ala Gln Leu Tyr Cys His Ser Ile Met Glu 2025 2 342 PRT Homo Sapiens 2 Glu Glu Glu Thr Arg Glu Leu Gln Ser Leu AlaAla Ala Val Val Pro 1 5 10 15 Ser Ala Gln Thr Leu Lys Ile Thr Asp PheSer Phe Ser Asp Phe Glu 20 25 30 Leu Ser Asp Leu Glu Thr Ala Leu Cys ThrIle Arg Met Phe Thr Asp 35 40 45 Leu Asn Leu Val Gln Asn Phe Gln Met LysHis Glu Val Leu Cys Arg 50 55 60 Trp Ile Leu Ser Val Lys Lys Asn Tyr ArgLys Asn Val Ala Tyr His 65 70 75 80 Asn Trp Arg His Ala Phe Asn Thr AlaGln Cys Met Phe Ala Ala Leu 85 90 95 Lys Ala Gly Lys Ile Gln Asn Lys LeuThr Asp Leu Glu Ile Leu Ala 100 105 110 Leu Leu Ile Ala Ala Leu Ser HisAsp Leu Asp His Arg Gly Val Asn 115 120 125 Asn Ser Tyr Ile Gln Arg SerGlu His Pro Leu Ala Gln Leu Tyr Cys 130 135 140 His Ser Ile Met Glu HisHis His Phe Asp Gln Cys Leu Met Ile Leu 145 150 155 160 Asn Ser Pro GlyAsn Gln Ile Leu Ser Gly Leu Ser Ile Glu Glu Tyr 165 170 175 Lys Thr ThrLeu Lys Ile Ile Lys Gln Ala Ile Leu Ala Thr Asp Leu 180 185 190 Ala LeuTyr Ile Lys Arg Arg Gly Glu Phe Phe Glu Leu Ile Arg Lys 195 200 205 AsnGln Phe Asn Leu Glu Asp Pro His Gln Lys Glu Leu Phe Leu Ala 210 215 220Met Leu Met Thr Ala Cys Asp Leu Ser Ala Ile Thr Lys Pro Trp Pro 225 230235 240 Ile Gln Gln Arg Ile Ala Glu Leu Val Ala Thr Glu Phe Phe Asp Gln245 250 255 Gly Asp Arg Glu Arg Lys Glu Leu Asn Ile Glu Pro Thr Asp LeuMet 260 265 270 Asn Arg Glu Lys Lys Asn Lys Ile Pro Ser Met Gln Val GlyPhe Ile 275 280 285 Asp Ala Ile Cys Leu Gln Leu Tyr Glu Ala Leu Thr HisVal Ser Glu 290 295 300 Asp Cys Phe Pro Leu Leu Asp Gly Cys Arg Lys AsnArg Gln Lys Trp 305 310 315 320 Gln Ala Leu Ala Glu Gln Gln Glu Lys MetLeu Ile Asn Gly Glu Ser 325 330 335 Gly Gln Ala Lys Arg Asn 340 3 874PRT Homo Sapiens 3 Glu Arg Ala Gly Pro Ser Phe Gly Gln Gln Arg Gln GlnGln Gln Pro 1 5 10 15 Gln Gln Gln Lys Gln Gln Gln Arg Asp Gln Asp SerVal Glu Ala Trp 20 25 30 Leu Asp Asp His Trp Asp Phe Thr Phe Ser Tyr PheVal Arg Lys Ala 35 40 45 Thr Arg Glu Met Val Asn Ala Trp Phe Ala Glu ArgVal His Thr Ile 50 55 60 Pro Val Cys Lys Glu Gly Ile Arg Gly His Thr GluSer Cys Ser Cys 65 70 75 80 Pro Leu Gln Gln Ser Pro Arg Ala Asp Asn SerVal Pro Gly Thr Pro 85 90 95 Thr Arg Lys Ile Ser Ala Ser Glu Phe Asp ArgPro Leu Arg Pro Ile 100 105 110 Val Val Lys Asp Ser Glu Gly Thr Val SerPhe Leu Ser Asp Ser Glu 115 120 125 Lys Lys Glu Gln Met Pro Leu Thr ProPro Arg Phe Asp His Asp Glu 130 135 140 Gly Asp Gln Cys Ser Arg Leu LeuGlu Leu Val Lys Asp Ile Ser Ser 145 150 155 160 His Leu Asp Val Thr AlaLeu Cys His Lys Ile Phe Leu His Ile His 165 170 175 Gly Leu Ile Ser AlaAsp Arg Tyr Ser Leu Phe Leu Val Cys Glu Asp 180 185 190 Ser Ser Asn AspLys Phe Leu Ile Ser Arg Leu Phe Asp Val Ala Glu 195 200 205 Gly Ser ThrLeu Glu Glu Val Ser Asn Asn Cys Ile Arg Leu Glu Trp 210 215 220 Asn LysGly Ile Val Gly His Val Ala Ala Leu Gly Glu Pro Leu Asn 225 230 235 240Ile Lys Asp Ala Tyr Glu Asp Pro Arg Phe Asn Ala Glu Val Asp Gln 245 250255 Ile Thr Gly Tyr Lys Thr Gln Ser Ile Leu Cys Met Pro Ile Lys Asn 260265 270 His Arg Glu Glu Val Val Gly Val Ala Gln Ala Ile Asn Lys Lys Ser275 280 285 Gly Asn Gly Gly Thr Phe Thr Glu Lys Asp Glu Lys Asp Phe AlaAla 290 295 300 Tyr Leu Ala Phe Cys Gly Ile Val Leu His Asn Ala Gln LeuTyr Glu 305 310 315 320 Thr Ser Leu Leu Glu Asn Lys Arg Asn Gln Val LeuLeu Asp Leu Ala 325 330 335 Ser Leu Ile Phe Glu Glu Gln Gln Ser Leu GluVal Ile Leu Lys Lys 340 345 350 Ile Ala Ala Thr Ile Ile Ser Phe Met GlnVal Gln Lys Cys Thr Ile 355 360 365 Phe Ile Val Asp Glu Asp Cys Ser AspSer Phe Ser Ser Val Phe His 370 375 380 Met Glu Cys Glu Glu Leu Glu LysSer Ser Asp Thr Leu Thr Arg Glu 385 390 395 400 His Asp Ala Asn Lys IleAsn Tyr Met Tyr Ala Gln Tyr Val Lys Asn 405 410 415 Thr Met Glu Pro LeuAsn Ile Pro Asp Val Ser Lys Asp Lys Arg Phe 420 425 430 Pro Trp Thr ThrGlu Asn Thr Gly Asn Val Asn Gln Gln Cys Ile Arg 435 440 445 Ser Leu LeuCys Thr Pro Ile Lys Asn Gly Lys Lys Asn Lys Val Ile 450 455 460 Gly ValCys Gln Leu Val Asn Lys Met Glu Glu Asn Thr Gly Lys Val 465 470 475 480Lys Pro Phe Asn Arg Asn Asp Glu Gln Phe Leu Glu Ala Phe Val Ile 485 490495 Phe Cys Gly Leu Gly Ile Gln Asn Thr Gln Met Tyr Glu Ala Val Glu 500505 510 Arg Ala Met Ala Lys Gln Met Val Thr Leu Glu Val Leu Ser Tyr His515 520 525 Ala Ser Ala Ala Glu Glu Glu Thr Arg Glu Leu Gln Ser Leu AlaAla 530 535 540 Ala Val Val Pro Ser Ala Gln Thr Leu Lys Ile Thr Asp PheSer Phe 545 550 555 560 Ser Asp Phe Glu Leu Ser Asp Leu Glu Thr Ala LeuCys Thr Ile Arg 565 570 575 Met Phe Thr Asp Leu Asn Leu Val Gln Asn PheGln Met Lys His Glu 580 585 590 Val Leu Cys Arg Trp Ile Leu Ser Val LysLys Asn Tyr Arg Lys Asn 595 600 605 Val Ala Tyr His Asn Trp Arg His AlaPhe Asn Thr Ala Gln Cys Met 610 615 620 Phe Ala Ala Leu Lys Ala Gly LysIle Gln Asn Lys Leu Thr Asp Leu 625 630 635 640 Glu Ile Leu Ala Leu LeuIle Ala Ala Leu Ser His Asp Leu Asp His 645 650 655 Arg Gly Val Asn AsnSer Tyr Ile Gln Arg Ser Glu His Pro Leu Ala 660 665 670 Gln Leu Tyr CysHis Ser Ile Met Glu His His His Phe Asp Gln Cys 675 680 685 Leu Met IleLeu Asn Ser Pro Gly Asn Gln Ile Leu Ser Gly Leu Ser 690 695 700 Ile GluGlu Tyr Lys Thr Thr Leu Lys Ile Ile Lys Gln Ala Ile Leu 705 710 715 720Ala Thr Asp Leu Ala Leu Tyr Ile Lys Arg Arg Gly Glu Phe Phe Glu 725 730735 Leu Ile Arg Lys Asn Gln Phe Asn Leu Glu Asp Pro His Gln Lys Glu 740745 750 Leu Phe Leu Ala Met Leu Met Thr Ala Cys Asp Leu Ser Ala Ile Thr755 760 765 Lys Pro Trp Pro Ile Gln Gln Arg Ile Ala Glu Leu Val Ala ThrGlu 770 775 780 Phe Phe Asp Gln Gly Asp Arg Glu Arg Lys Glu Leu Asn IleGlu Pro 785 790 795 800 Thr Asp Leu Met Asn Arg Glu Lys Lys Asn Lys IlePro Ser Met Gln 805 810 815 Val Gly Phe Ile Asp Ala Ile Cys Leu Gln LeuTyr Glu Ala Leu Thr 820 825 830 His Val Ser Glu Asp Cys Phe Pro Leu LeuAsp Gly Cys Arg Lys Asn 835 840 845 Arg Gln Lys Trp Gln Ala Leu Ala GluGln Gln Glu Lys Met Leu Ile 850 855 860 Asn Gly Glu Ser Gly Gln Ala LysArg Asn 865 870 4 27 PRT Homo Sapiens 4 His Pro Gly Val Ser Asn Gln PheLeu Ile Asn Thr Asn Ser Glu Leu 1 5 10 15 Ala Leu Met Tyr Asn Asp GluSer Val Leu Glu 20 25 5 326 PRT Homo Sapiens 5 Glu Glu Glu Thr Arg GluLeu Gln Ser Leu Ala Ala Ala Val Val Pro 1 5 10 15 Ser Ala Gln Thr LeuLys Ile Thr Asp Phe Ser Phe Ser Asp Phe Glu 20 25 30 Leu Ser Asp Leu GluThr Ala Leu Cys Thr Ile Arg Met Phe Thr Asp 35 40 45 Leu Asn Leu Val GlnAsn Phe Gln Met Lys His Glu Val Leu Cys Arg 50 55 60 Trp Ile Leu Ser ValLys Lys Asn Tyr Arg Lys Asn Val Ala Tyr His 65 70 75 80 Asn Trp Arg HisAla Phe Asn Thr Ala Gln Cys Met Phe Ala Ala Leu 85 90 95 Lys Ala Gly LysIle Gln Asn Lys Leu Thr Asp Leu Glu Ile Leu Ala 100 105 110 Leu Leu IleAla Ala Leu Ser His Asp Leu Asp His Pro Gly Val Ser 115 120 125 Asn GlnPhe Leu Ile Asn Thr Asn Ser Glu Leu Ala Leu Met Tyr Asn 130 135 140 AspGlu Ser Val Leu Glu His His His Phe Asp Gln Cys Leu Met Ile 145 150 155160 Leu Asn Ser Pro Gly Asn Gln Ile Leu Ser Gly Leu Ser Ile Glu Glu 165170 175 Tyr Lys Thr Thr Leu Lys Ile Ile Lys Gln Ala Ile Leu Ala Thr Asp180 185 190 Leu Ala Leu Tyr Ile Lys Arg Arg Gly Glu Phe Phe Glu Leu IleArg 195 200 205 Lys Asn Gln Phe Asn Leu Glu Asp Pro His Gln Lys Glu LeuPhe Leu 210 215 220 Ala Met Leu Met Thr Ala Cys Asp Leu Ser Ala Ile ThrLys Pro Trp 225 230 235 240 Pro Ile Gln Gln Arg Ile Ala Glu Leu Val AlaThr Glu Phe Phe Asp 245 250 255 Gln Gly Asp Arg Glu Arg Lys Glu Leu AsnIle Glu Pro Thr Asp Leu 260 265 270 Met Asn Arg Glu Lys Lys Asn Lys IlePro Ser Met Gln Val Gly Phe 275 280 285 Ile Asp Ala Ile Cys Leu Gln LeuTyr Glu Ala Leu Thr His Val Ser 290 295 300 Glu Asp Cys Phe Pro Leu LeuAsp Gly Cys Arg Lys Asn Arg Gln Lys 305 310 315 320 Trp Gln Ala Leu AlaGlu 325 6 858 PRT Homo Sapiens 6 Glu Arg Ala Gly Pro Ser Phe Gly Gln GlnArg Gln Gln Gln Gln Pro 1 5 10 15 Gln Gln Gln Lys Gln Gln Gln Arg AspGln Asp Ser Val Glu Ala Trp 20 25 30 Leu Asp Asp His Trp Asp Phe Thr PheSer Tyr Phe Val Arg Lys Ala 35 40 45 Thr Arg Glu Met Val Asn Ala Trp PheAla Glu Arg Val His Thr Ile 50 55 60 Pro Val Cys Lys Glu Gly Ile Arg GlyHis Thr Glu Ser Cys Ser Cys 65 70 75 80 Pro Leu Gln Gln Ser Pro Arg AlaAsp Asn Ser Val Pro Gly Thr Pro 85 90 95 Thr Arg Lys Ile Ser Ala Ser GluPhe Asp Arg Pro Leu Arg Pro Ile 100 105 110 Val Val Lys Asp Ser Glu GlyThr Val Ser Phe Leu Ser Asp Ser Glu 115 120 125 Lys Lys Glu Gln Met ProLeu Thr Pro Pro Arg Phe Asp His Asp Glu 130 135 140 Gly Asp Gln Cys SerArg Leu Leu Glu Leu Val Lys Asp Ile Ser Ser 145 150 155 160 His Leu AspVal Thr Ala Leu Cys His Lys Ile Phe Leu His Ile His 165 170 175 Gly LeuIle Ser Ala Asp Arg Tyr Ser Leu Phe Leu Val Cys Glu Asp 180 185 190 SerSer Asn Asp Lys Phe Leu Ile Ser Arg Leu Phe Asp Val Ala Glu 195 200 205Gly Ser Thr Leu Glu Glu Val Ser Asn Asn Cys Ile Arg Leu Glu Trp 210 215220 Asn Lys Gly Ile Val Gly His Val Ala Ala Leu Gly Glu Pro Leu Asn 225230 235 240 Ile Lys Asp Ala Tyr Glu Asp Pro Arg Phe Asn Ala Glu Val AspGln 245 250 255 Ile Thr Gly Tyr Lys Thr Gln Ser Ile Leu Cys Met Pro IleLys Asn 260 265 270 His Arg Glu Glu Val Val Gly Val Ala Gln Ala Ile AsnLys Lys Ser 275 280 285 Gly Asn Gly Gly Thr Phe Thr Glu Lys Asp Glu LysAsp Phe Ala Ala 290 295 300 Tyr Leu Ala Phe Cys Gly Ile Val Leu His AsnAla Gln Leu Tyr Glu 305 310 315 320 Thr Ser Leu Leu Glu Asn Lys Arg AsnGln Val Leu Leu Asp Leu Ala 325 330 335 Ser Leu Ile Phe Glu Glu Gln GlnSer Leu Glu Val Ile Leu Lys Lys 340 345 350 Ile Ala Ala Thr Ile Ile SerPhe Met Gln Val Gln Lys Cys Thr Ile 355 360 365 Phe Ile Val Asp Glu AspCys Ser Asp Ser Phe Ser Ser Val Phe His 370 375 380 Met Glu Cys Glu GluLeu Glu Lys Ser Ser Asp Thr Leu Thr Arg Glu 385 390 395 400 His Asp AlaAsn Lys Ile Asn Tyr Met Tyr Ala Gln Tyr Val Lys Asn 405 410 415 Thr MetGlu Pro Leu Asn Ile Pro Asp Val Ser Lys Asp Lys Arg Phe 420 425 430 ProTrp Thr Thr Glu Asn Thr Gly Asn Val Asn Gln Gln Cys Ile Arg 435 440 445Ser Leu Leu Cys Thr Pro Ile Lys Asn Gly Lys Lys Asn Lys Val Ile 450 455460 Gly Val Cys Gln Leu Val Asn Lys Met Glu Glu Asn Thr Gly Lys Val 465470 475 480 Lys Pro Phe Asn Arg Asn Asp Glu Gln Phe Leu Glu Ala Phe ValIle 485 490 495 Phe Cys Gly Leu Gly Ile Gln Asn Thr Gln Met Tyr Glu AlaVal Glu 500 505 510 Arg Ala Met Ala Lys Gln Met Val Thr Leu Glu Val LeuSer Tyr His 515 520 525 Ala Ser Ala Ala Glu Glu Glu Thr Arg Glu Leu GlnSer Leu Ala Ala 530 535 540 Ala Val Val Pro Ser Ala Gln Thr Leu Lys IleThr Asp Phe Ser Phe 545 550 555 560 Ser Asp Phe Glu Leu Ser Asp Leu GluThr Ala Leu Cys Thr Ile Arg 565 570 575 Met Phe Thr Asp Leu Asn Leu ValGln Asn Phe Gln Met Lys His Glu 580 585 590 Val Leu Cys Arg Trp Ile LeuSer Val Lys Lys Asn Tyr Arg Lys Asn 595 600 605 Val Ala Tyr His Asn TrpArg His Ala Phe Asn Thr Ala Gln Cys Met 610 615 620 Phe Ala Ala Leu LysAla Gly Lys Ile Gln Asn Lys Leu Thr Asp Leu 625 630 635 640 Glu Ile LeuAla Leu Leu Ile Ala Ala Leu Ser His Asp Leu Asp His 645 650 655 Pro GlyVal Ser Asn Gln Phe Leu Ile Asn Thr Asn Ser Glu Leu Ala 660 665 670 LeuMet Tyr Asn Asp Glu Ser Val Leu Glu His His His Phe Asp Gln 675 680 685Cys Leu Met Ile Leu Asn Ser Pro Gly Asn Gln Ile Leu Ser Gly Leu 690 695700 Ser Ile Glu Glu Tyr Lys Thr Thr Leu Lys Ile Ile Lys Gln Ala Ile 705710 715 720 Leu Ala Thr Asp Leu Ala Leu Tyr Ile Lys Arg Arg Gly Glu PhePhe 725 730 735 Glu Leu Ile Arg Lys Asn Gln Phe Asn Leu Glu Asp Pro HisGln Lys 740 745 750 Glu Leu Phe Leu Ala Met Leu Met Thr Ala Cys Asp LeuSer Ala Ile 755 760 765 Thr Lys Pro Trp Pro Ile Gln Gln Arg Ile Ala GluLeu Val Ala Thr 770 775 780 Glu Phe Phe Asp Gln Gly Asp Arg Glu Arg LysGlu Leu Asn Ile Glu 785 790 795 800 Pro Thr Asp Leu Met Asn Arg Glu LysLys Asn Lys Ile Pro Ser Met 805 810 815 Gln Val Gly Phe Ile Asp Ala IleCys Leu Gln Leu Tyr Glu Ala Leu 820 825 830 Thr His Val Ser Glu Asp CysPhe Pro Leu Leu Asp Gly Cys Arg Lys 835 840 845 Asn Arg Gln Lys Trp GlnAla Leu Ala Glu 850 855 7 34 DNA Homo Sapiens 7 cgtgaattca tggaggaagaaacaagagag ctac 34 8 42 DNA Homo Sapiens 8 cgttctagac tatcagttccgcttggcctg gccgctttcc cc 42 9 79 DNA Homo Sapiens 9 cgtgaattcatgcatcatca tcatcatcat cttctggttc cgcgtggatc tgcgcccgag 60 gaagaaacaagagagctac 79 10 72 DNA Homo Sapiens 10 caaagaaagt tctgaatttg tgttgatgagaaactgattg gagactccag gatgatccaa 60 atcgtggctt ag 72 11 72 DNA HomoSapiens 11 atcaacacaa attcagaact tgctttgatg tataatgatg aatctgtgttggaacaccat 60 cattttgacc ag 72 12 39 DNA Homo Sapiens 12 cgttctagactatcattctg caagggcctg ccatttctg 39 13 31 DNA Homo Sapiens 13 cgtcatatggaggaagaaac aagagagcta c 31 14 39 DNA Homo Sapiens 14 cgtctcgagctatcattctg caagggcctg ccatttctg 39

1. A crystal of phosphodiesterase 5 (PDE5).
 2. The crystal of PDE5according to claim 1, wherein the crystal is soakable.
 3. The crystal ofPDE5 according to any one of claims 1 or 2, wherein said PDE5 is from amammal.
 4. The crystal of PDE5 according to any one of claims 1 to 3,wherein said PDE5 is from a human.
 5. The crystal of PDE5 according toany one of claims 1 to 4, wherein said PDE5 is an isoform selected fromthe group including PDE5A1, PDE5A2, PDE5A3 and PDE5A4.
 6. The crystal ofPDE5 according to any one of claims 1 to 5, wherein said PDE5 comprisesSEQ ID NO: 1 or a homologue, fragment, variant, analogue or derivativethereof.
 7. The crystal of PDE5 according to any one of claims 1 to 6,wherein said PDE5 comprises SEQ ID NO: 4 or a homologue, fragment,variant, analogue or derivative thereof.
 8. The crystal of PDE5according to any one of claims 1 to 7, wherein said PDE5 comprises SEQID NO: 5 or a homologue, fragment, variant, analogue or derivativethereof.
 9. The crystal of PDE5 according to any one of claims 1 to 8,wherein said PDE5 comprises SEQ ID NO: 6 or a homologue, fragment,variant, analogue or derivative thereof.
 10. The crystal of PDE5according to any one of the claims 1 to 9 which is grown usingpolyethylene glycol as a precipitant.
 11. The crystal of PDE5 accordingto any one of claims 1 to 10 which is grown in a buffer in the pH rangeof 6.5 to 8.0.
 12. The crystal of PDE5 according to any one of theclaims 1 to 11 which is grown in the presence of an alcohol.
 13. Thecrystal of PDE5 according to any one of the claims 1 to 12 which isgrown in a solution containing HEPES buffer, polyethylene glycol 4000and iso-propanol.
 14. The crystal of PDE5 as defined in any one ofclaims 1 to 13, which has one or more of the following characteristics:(g) a space group C2; (h) unit cell dimensions a˜56 Å±1%, b˜77 Å±1%,c˜81 Å±1%, α=γ=90°, β=103°±1%; (i) 1 molecule per asymmetric unit; (J)comprises a PDE5 of a molecular weight of approximately 4 OkDa±2 kDa;(k) a calculated solvent content of approximately 47±5%; and (1) amonoclinic crystal system.
 15. The crystal of PDE5 as claimed in any oneof claims 1 to 14, wherein PDE5 has an active site within the thirdsub-domain of the protein which is bounded by Helices 15 (H15 813-824)and 14 (H14 772-797), the C-terminus of Helix 13 (H13 749-25 765), andthe C-terminus of Helix 11 (H11 706-721) along with the loop regionbetween Helices 11 and 12a (H12a 725-731) as shown in FIG.
 2. 16. Thecrystal of PDE5 as claimed in claim 15, wherein the active site iscapable of accommodating a pyrazolo-pyrimidinone.
 17. The crystal ofPDE5 as claimed in any one of the claims 1 to 16, wherein PDE5 has anactive site within the third sub-domain of the protein and comprises Leu765, Ala 767 and Ile 768 and one or more of Phe 820, Val 782, Phe 786,Tyr 612, Leu 804, Ala 779, Ala 783, Ile 813, Met 816 and Gln
 817. 18.The crystal of PDE5 as claimed in claim 17, wherein the active site iscapable of accommodating a ligand or inhibitor.
 19. The crystal of PDE5as claimed in any one of the claims 1 to 18, wherein said PDE5 has athree-dimensional structure characterised by the atomic co-ordinates setout in Table 4 or a derivative set as expressed in any reference frame.20. A heavy atom derivative of the crystal of PDE5 as claimed in any oneof the claims 1 to
 19. 21. The crystal of PDE5 as claimed in any one ofclaims 1 to 20, wherein a PDE5 ligand has been soaked in.
 22. Thecrystal of PDE5 as claimed in claim 22, wherein said PDE5 ligand is aPDE5 inhibitor.
 23. The crystal of PDE5 as claimed in claim 22, whereinsaid PDE5 inhibitor is a pyrazolo-pyrimidinone.
 24. The crystal of PDE5as claimed in any one of claims 21 to 23, wherein said PDE5 has athree-dimensional structure characterised by the atomic co-ordinates setout in Table 5 or a derivative set as expressed in any reference frame.25. Use of the atomic co-ordinates determined from the crystal of PDE5according to any one of claims 1 to 24 for deriving a three-dimensionalstructure of a PDE5 or a mutant, derivative, variant, analogue,homologue, sub-domain or fragment thereof.
 26. Use according to claim25, wherein the PDE5 sub-domain is the catalytic domain.
 27. Use of thethree-dimensional structure of PDE5 as derivable according to one ofclaim 25 or claim 26 to computationally or otherwise evaluate thebinding interactions of a chemical compound with an active site on PDE5.28. Use of the three-dimensional structure of PDE5 as derivableaccording to claim 27 to design a compound capable of associating withPDE5.
 29. Use according to claim 27 or claim 28, wherein the compound isa PDE5 ligand.
 30. Use according to claim 29, wherein said compound is aPDE5 inhibitor.
 31. Use according to claim 30, wherein said PDE5inhibitor is a pyrazolo-pyrimidinone.
 32. A method of selecting acompound capable of associating with PDE5 from a group of potential PDE5ligand compounds comprising the following steps: i. soaking the crystalof PDE5 according to any one of claims 1 to 19 in a solution containinga potential PDE5 ligand compound; ii. determining the three-dimensionalstructure from the soaked crystal; and iii. assessing whether thecompound is bound to PDE5.
 33. A compound selected by the use accordingto claim
 32. 34. A compound designed by the use according to any one ofclaims 28 to 31 or identified by the method of claim
 32. 35. Thecompound according to claim 34, which is a PDE5 inhibitor.
 36. A methodof selecting a PDE5 ligand from a group of potential PDE5 ligands,comprising the following steps: (a) computationally creating athree-dimensional representation of the structure of 30 PDE5 asderivable according to any one of claim 25 or claim 26, and athree-dimensional representation of the structure of the potential PDE5ligand; (b) co-displaying the three-dimensional representation of thepotential PDE5 ligand with the three-dimensional representation of thePDE5 structure; and (c) assessing whether the three-dimensionalrepresentation of the potential PDE5 ligand fits the three-dimensionalrepresentation of an active site of the PDE5 structure.
 37. The methodaccording to claim 36, further comprising the following steps: (d)incorporating the potential PDE5 ligand in a biological PDE5 activityassay; and (e) determining whether the potential PDE5 ligand modulatesPDE5 activity in said assay.
 38. The method according to any one ofclaim 36 or claim 37 wherein said potential PDE5 ligand is a potentialPDE5 inhibitor compound and said potential PDE5 inhibitor compoundinhibits PDE5 activity.
 39. A PDE5 ligand selected by the method of anyone of claims 36 to
 38. 40. Use of a PDE5 ligand according to claim 39as a pharmaceutical.
 41. A pharmaceutical composition comprising one ormore PDE5 ligands according to claim 39 and one or more pharmaceuticallyacceptable excipients.
 42. Use of a PDE5 ligand according to claim 39 inthe manufacture of a medicament for the prophylaxis or treatment of acondition, disease, disorder or dysfunction where the inhibition of PDE5is prophylactically or therapeutically beneficial.
 43. Use according toclaim 42, wherein said disorder is a mammalian sexual disorder.
 44. Useof the atomic co-ordinates determined from the crystal of PDE5 accordingto any one of claims 1 to 24, to solve the crystal structure of amutant, derivative, fragment, variant, analogue, homologue or complex ofPDE5.
 45. Use of the atomic co-ordinates determined from the crystal ofPDE5 according to any one of claims 1 to 24, to produce a model of thethree-dimensional structure of PDE5-related proteins.
 46. Use of thethree-dimensional structure of PDE5 as derivable according to any one ofclaim 25 or claim 26 to design site-directed mutants that mimic otherPDE5 isoforms or variants thereof.
 47. A method of soaking a chemicalcompound into a crystal according to any one of claims 1 to 20comprising the following steps: a) incubating the crystal in an aqueousstabilising solution comprising buffer lo and polyethylene glycol; b)combining the chemical compound with the stabilising solution; and c)optionally adding a cryo-protectant to the stabilising solution.